Eintrag weiter verarbeiten
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction
Gespeichert in:
| Zeitschriftentitel: | Acta Crystallographica Section D Biological Crystallography |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Acta Crystallographica Section D Biological Crystallography, 68, 2012, 12, S. 1660-1670 |
| Format: | E-Article |
| Sprache: | Unbestimmt |
| veröffentlicht: |
International Union of Crystallography (IUCr)
|
| Schlagwörter: |
| author_facet |
Timofeev, Vladimir Smirnova, Evgenia Chupova, Larisa Esipov, Roman Kuranova, Inna Timofeev, Vladimir Smirnova, Evgenia Chupova, Larisa Esipov, Roman Kuranova, Inna |
|---|---|
| author |
Timofeev, Vladimir Smirnova, Evgenia Chupova, Larisa Esipov, Roman Kuranova, Inna |
| spellingShingle |
Timofeev, Vladimir Smirnova, Evgenia Chupova, Larisa Esipov, Roman Kuranova, Inna Acta Crystallographica Section D Biological Crystallography X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction General Medicine Structural Biology |
| author_sort |
timofeev, vladimir |
| spelling |
Timofeev, Vladimir Smirnova, Evgenia Chupova, Larisa Esipov, Roman Kuranova, Inna 0907-4449 International Union of Crystallography (IUCr) General Medicine Structural Biology http://dx.doi.org/10.1107/s0907444912040206 <jats:p>Structures of recombinant phosphopantetheine adenylyltransferase (PPAT) from<jats:italic>Mycobacterium tuberculosis</jats:italic>(PPATMt) in the apo form and in complex with the substrate ATP were determined at 1.62 and 1.70 Å resolution, respectively, using crystals grown in microgravity by the counter-diffusion method. The ATP molecule of the PPATMt–ATP complex was located with full occupancy in the active-site cavity. Comparison of the solved structures with previously determined structures of PPATMt complexed with the reaction product dephosphocoenzyme A (dPCoA) and the feedback inhibitor coenzyme A (CoA) was performed using superposition on C<jats:sup>α</jats:sup>atoms. The peculiarities of the arrangement of the ligands in the active-site cavity of PPATMt are described. The conformational states of the PPAT molecule in the consequent steps of the catalyzed reaction in the apo enzyme and the enzyme–substrate and enzyme–product complexes are characterized. It is shown that the binding of ATP and dPCoA induces the rearrangement of a short part of the polypeptide chain restricting the active-site cavity in the subunits of the hexameric enzyme molecule. The changes in the quaternary structure caused by this rearrangement are accompanied by a variation of the size of the inner water-filled channel which crosses the PPAT molecule along the threefold axis of the hexamer. The molecular mechanism of the observed changes is described.</jats:p> X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from<i>Mycobacterium tuberculosis</i>during the catalyzed reaction Acta Crystallographica Section D Biological Crystallography |
| doi_str_mv |
10.1107/s0907444912040206 |
| facet_avail |
Online |
| finc_class_facet |
Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEwNy9zMDkwNzQ0NDkxMjA0MDIwNg |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEwNy9zMDkwNzQ0NDkxMjA0MDIwNg |
| institution |
DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 |
| imprint |
International Union of Crystallography (IUCr), 2012 |
| imprint_str_mv |
International Union of Crystallography (IUCr), 2012 |
| issn |
0907-4449 |
| issn_str_mv |
0907-4449 |
| language |
Undetermined |
| mega_collection |
International Union of Crystallography (IUCr) (CrossRef) |
| match_str |
timofeev2012xraystudyoftheconformationalchangesinthemoleculeofphosphopantetheineadenylyltransferasefrommycobacteriumtuberculosisduringthecatalyzedreaction |
| publishDateSort |
2012 |
| publisher |
International Union of Crystallography (IUCr) |
| recordtype |
ai |
| record_format |
ai |
| series |
Acta Crystallographica Section D Biological Crystallography |
| source_id |
49 |
| title |
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_unstemmed |
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_full |
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_fullStr |
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_full_unstemmed |
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_short |
X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_sort |
x-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from<i>mycobacterium tuberculosis</i>during the catalyzed reaction |
| topic |
General Medicine Structural Biology |
| url |
http://dx.doi.org/10.1107/s0907444912040206 |
| publishDate |
2012 |
| physical |
1660-1670 |
| description |
<jats:p>Structures of recombinant phosphopantetheine adenylyltransferase (PPAT) from<jats:italic>Mycobacterium tuberculosis</jats:italic>(PPATMt) in the apo form and in complex with the substrate ATP were determined at 1.62 and 1.70 Å resolution, respectively, using crystals grown in microgravity by the counter-diffusion method. The ATP molecule of the PPATMt–ATP complex was located with full occupancy in the active-site cavity. Comparison of the solved structures with previously determined structures of PPATMt complexed with the reaction product dephosphocoenzyme A (dPCoA) and the feedback inhibitor coenzyme A (CoA) was performed using superposition on C<jats:sup>α</jats:sup>atoms. The peculiarities of the arrangement of the ligands in the active-site cavity of PPATMt are described. The conformational states of the PPAT molecule in the consequent steps of the catalyzed reaction in the apo enzyme and the enzyme–substrate and enzyme–product complexes are characterized. It is shown that the binding of ATP and dPCoA induces the rearrangement of a short part of the polypeptide chain restricting the active-site cavity in the subunits of the hexameric enzyme molecule. The changes in the quaternary structure caused by this rearrangement are accompanied by a variation of the size of the inner water-filled channel which crosses the PPAT molecule along the threefold axis of the hexamer. The molecular mechanism of the observed changes is described.</jats:p> |
| container_issue |
12 |
| container_start_page |
1660 |
| container_title |
Acta Crystallographica Section D Biological Crystallography |
| container_volume |
68 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792342188921716743 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T16:31:51.256Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=X-ray+study+of+the+conformational+changes+in+the+molecule+of+phosphopantetheine+adenylyltransferase+fromMycobacterium+tuberculosisduring+the+catalyzed+reaction&rft.date=2012-12-01&genre=article&issn=0907-4449&volume=68&issue=12&spage=1660&epage=1670&pages=1660-1670&jtitle=Acta+Crystallographica+Section+D+Biological+Crystallography&atitle=X-ray+study+of+the+conformational+changes+in+the+molecule+of+phosphopantetheine+adenylyltransferase+from%3Ci%3EMycobacterium+tuberculosis%3C%2Fi%3Eduring+the+catalyzed+reaction&aulast=Kuranova&aufirst=Inna&rft_id=info%3Adoi%2F10.1107%2Fs0907444912040206&rft.language%5B0%5D=und |
| SOLR | |
| _version_ | 1792342188921716743 |
| author | Timofeev, Vladimir, Smirnova, Evgenia, Chupova, Larisa, Esipov, Roman, Kuranova, Inna |
| author_facet | Timofeev, Vladimir, Smirnova, Evgenia, Chupova, Larisa, Esipov, Roman, Kuranova, Inna, Timofeev, Vladimir, Smirnova, Evgenia, Chupova, Larisa, Esipov, Roman, Kuranova, Inna |
| author_sort | timofeev, vladimir |
| container_issue | 12 |
| container_start_page | 1660 |
| container_title | Acta Crystallographica Section D Biological Crystallography |
| container_volume | 68 |
| description | <jats:p>Structures of recombinant phosphopantetheine adenylyltransferase (PPAT) from<jats:italic>Mycobacterium tuberculosis</jats:italic>(PPATMt) in the apo form and in complex with the substrate ATP were determined at 1.62 and 1.70 Å resolution, respectively, using crystals grown in microgravity by the counter-diffusion method. The ATP molecule of the PPATMt–ATP complex was located with full occupancy in the active-site cavity. Comparison of the solved structures with previously determined structures of PPATMt complexed with the reaction product dephosphocoenzyme A (dPCoA) and the feedback inhibitor coenzyme A (CoA) was performed using superposition on C<jats:sup>α</jats:sup>atoms. The peculiarities of the arrangement of the ligands in the active-site cavity of PPATMt are described. The conformational states of the PPAT molecule in the consequent steps of the catalyzed reaction in the apo enzyme and the enzyme–substrate and enzyme–product complexes are characterized. It is shown that the binding of ATP and dPCoA induces the rearrangement of a short part of the polypeptide chain restricting the active-site cavity in the subunits of the hexameric enzyme molecule. The changes in the quaternary structure caused by this rearrangement are accompanied by a variation of the size of the inner water-filled channel which crosses the PPAT molecule along the threefold axis of the hexamer. The molecular mechanism of the observed changes is described.</jats:p> |
| doi_str_mv | 10.1107/s0907444912040206 |
| facet_avail | Online |
| finc_class_facet | Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEwNy9zMDkwNzQ0NDkxMjA0MDIwNg |
| imprint | International Union of Crystallography (IUCr), 2012 |
| imprint_str_mv | International Union of Crystallography (IUCr), 2012 |
| institution | DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1 |
| issn | 0907-4449 |
| issn_str_mv | 0907-4449 |
| language | Undetermined |
| last_indexed | 2024-03-01T16:31:51.256Z |
| match_str | timofeev2012xraystudyoftheconformationalchangesinthemoleculeofphosphopantetheineadenylyltransferasefrommycobacteriumtuberculosisduringthecatalyzedreaction |
| mega_collection | International Union of Crystallography (IUCr) (CrossRef) |
| physical | 1660-1670 |
| publishDate | 2012 |
| publishDateSort | 2012 |
| publisher | International Union of Crystallography (IUCr) |
| record_format | ai |
| recordtype | ai |
| series | Acta Crystallographica Section D Biological Crystallography |
| source_id | 49 |
| spelling | Timofeev, Vladimir Smirnova, Evgenia Chupova, Larisa Esipov, Roman Kuranova, Inna 0907-4449 International Union of Crystallography (IUCr) General Medicine Structural Biology http://dx.doi.org/10.1107/s0907444912040206 <jats:p>Structures of recombinant phosphopantetheine adenylyltransferase (PPAT) from<jats:italic>Mycobacterium tuberculosis</jats:italic>(PPATMt) in the apo form and in complex with the substrate ATP were determined at 1.62 and 1.70 Å resolution, respectively, using crystals grown in microgravity by the counter-diffusion method. The ATP molecule of the PPATMt–ATP complex was located with full occupancy in the active-site cavity. Comparison of the solved structures with previously determined structures of PPATMt complexed with the reaction product dephosphocoenzyme A (dPCoA) and the feedback inhibitor coenzyme A (CoA) was performed using superposition on C<jats:sup>α</jats:sup>atoms. The peculiarities of the arrangement of the ligands in the active-site cavity of PPATMt are described. The conformational states of the PPAT molecule in the consequent steps of the catalyzed reaction in the apo enzyme and the enzyme–substrate and enzyme–product complexes are characterized. It is shown that the binding of ATP and dPCoA induces the rearrangement of a short part of the polypeptide chain restricting the active-site cavity in the subunits of the hexameric enzyme molecule. The changes in the quaternary structure caused by this rearrangement are accompanied by a variation of the size of the inner water-filled channel which crosses the PPAT molecule along the threefold axis of the hexamer. The molecular mechanism of the observed changes is described.</jats:p> X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from<i>Mycobacterium tuberculosis</i>during the catalyzed reaction Acta Crystallographica Section D Biological Crystallography |
| spellingShingle | Timofeev, Vladimir, Smirnova, Evgenia, Chupova, Larisa, Esipov, Roman, Kuranova, Inna, Acta Crystallographica Section D Biological Crystallography, X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction, General Medicine, Structural Biology |
| title | X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_full | X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_fullStr | X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_full_unstemmed | X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_short | X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| title_sort | x-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase from<i>mycobacterium tuberculosis</i>during the catalyzed reaction |
| title_unstemmed | X-ray study of the conformational changes in the molecule of phosphopantetheine adenylyltransferase fromMycobacterium tuberculosisduring the catalyzed reaction |
| topic | General Medicine, Structural Biology |
| url | http://dx.doi.org/10.1107/s0907444912040206 |