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Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli
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| Zeitschriftentitel: | Acta Crystallographica Section F Structural Biology Communications |
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| Personen und Körperschaften: | , , , , , , , |
| In: | Acta Crystallographica Section F Structural Biology Communications, 76, 2020, 2, S. 86-93 |
| Format: | E-Article |
| Sprache: | Unbestimmt |
| veröffentlicht: |
International Union of Crystallography (IUCr)
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| Schlagwörter: |
| author_facet |
Yoshizawa, Takuya Fujita, Junso Terakado, Haruna Ozawa, Mayuki Kuroda, Natsuko Tanaka, Shun-ichi Uehara, Ryo Matsumura, Hiroyoshi Yoshizawa, Takuya Fujita, Junso Terakado, Haruna Ozawa, Mayuki Kuroda, Natsuko Tanaka, Shun-ichi Uehara, Ryo Matsumura, Hiroyoshi |
|---|---|
| author |
Yoshizawa, Takuya Fujita, Junso Terakado, Haruna Ozawa, Mayuki Kuroda, Natsuko Tanaka, Shun-ichi Uehara, Ryo Matsumura, Hiroyoshi |
| spellingShingle |
Yoshizawa, Takuya Fujita, Junso Terakado, Haruna Ozawa, Mayuki Kuroda, Natsuko Tanaka, Shun-ichi Uehara, Ryo Matsumura, Hiroyoshi Acta Crystallographica Section F Structural Biology Communications Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics |
| author_sort |
yoshizawa, takuya |
| spelling |
Yoshizawa, Takuya Fujita, Junso Terakado, Haruna Ozawa, Mayuki Kuroda, Natsuko Tanaka, Shun-ichi Uehara, Ryo Matsumura, Hiroyoshi 2053-230X International Union of Crystallography (IUCr) Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1107/s2053230x2000076x <jats:p>FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from <jats:italic>Klebsiella pneumoniae</jats:italic> (KpFtsZ) and <jats:italic>Escherichia coli</jats:italic> (EcFtsZ) were determined at 1.75 and 2.50 Å resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.</jats:p> Crystal structures of the cell-division protein FtsZ from <i>Klebsiella pneumoniae</i> and <i>Escherichia coli</i> Acta Crystallographica Section F Structural Biology Communications |
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Acta Crystallographica Section F Structural Biology Communications |
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| title |
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_unstemmed |
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_full |
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_fullStr |
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_full_unstemmed |
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_short |
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_sort |
crystal structures of the cell-division protein ftsz from <i>klebsiella pneumoniae</i> and <i>escherichia coli</i> |
| topic |
Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1107/s2053230x2000076x |
| publishDate |
2020 |
| physical |
86-93 |
| description |
<jats:p>FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from <jats:italic>Klebsiella pneumoniae</jats:italic> (KpFtsZ) and <jats:italic>Escherichia coli</jats:italic> (EcFtsZ) were determined at 1.75 and 2.50 Å resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.</jats:p> |
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| author | Yoshizawa, Takuya, Fujita, Junso, Terakado, Haruna, Ozawa, Mayuki, Kuroda, Natsuko, Tanaka, Shun-ichi, Uehara, Ryo, Matsumura, Hiroyoshi |
| author_facet | Yoshizawa, Takuya, Fujita, Junso, Terakado, Haruna, Ozawa, Mayuki, Kuroda, Natsuko, Tanaka, Shun-ichi, Uehara, Ryo, Matsumura, Hiroyoshi, Yoshizawa, Takuya, Fujita, Junso, Terakado, Haruna, Ozawa, Mayuki, Kuroda, Natsuko, Tanaka, Shun-ichi, Uehara, Ryo, Matsumura, Hiroyoshi |
| author_sort | yoshizawa, takuya |
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| description | <jats:p>FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from <jats:italic>Klebsiella pneumoniae</jats:italic> (KpFtsZ) and <jats:italic>Escherichia coli</jats:italic> (EcFtsZ) were determined at 1.75 and 2.50 Å resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.</jats:p> |
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| imprint | International Union of Crystallography (IUCr), 2020 |
| imprint_str_mv | International Union of Crystallography (IUCr), 2020 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161 |
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| mega_collection | International Union of Crystallography (IUCr) (CrossRef) |
| physical | 86-93 |
| publishDate | 2020 |
| publishDateSort | 2020 |
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| spelling | Yoshizawa, Takuya Fujita, Junso Terakado, Haruna Ozawa, Mayuki Kuroda, Natsuko Tanaka, Shun-ichi Uehara, Ryo Matsumura, Hiroyoshi 2053-230X International Union of Crystallography (IUCr) Condensed Matter Physics Genetics Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1107/s2053230x2000076x <jats:p>FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from <jats:italic>Klebsiella pneumoniae</jats:italic> (KpFtsZ) and <jats:italic>Escherichia coli</jats:italic> (EcFtsZ) were determined at 1.75 and 2.50 Å resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.</jats:p> Crystal structures of the cell-division protein FtsZ from <i>Klebsiella pneumoniae</i> and <i>Escherichia coli</i> Acta Crystallographica Section F Structural Biology Communications |
| spellingShingle | Yoshizawa, Takuya, Fujita, Junso, Terakado, Haruna, Ozawa, Mayuki, Kuroda, Natsuko, Tanaka, Shun-ichi, Uehara, Ryo, Matsumura, Hiroyoshi, Acta Crystallographica Section F Structural Biology Communications, Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli, Condensed Matter Physics, Genetics, Biochemistry, Structural Biology, Biophysics |
| title | Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_full | Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_fullStr | Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_full_unstemmed | Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_short | Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| title_sort | crystal structures of the cell-division protein ftsz from <i>klebsiella pneumoniae</i> and <i>escherichia coli</i> |
| title_unstemmed | Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli |
| topic | Condensed Matter Physics, Genetics, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1107/s2053230x2000076x |