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Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes
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| Zeitschriftentitel: | IUCrJ |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | IUCrJ, 7, 2020, 3, S. 557-565 |
| Format: | E-Article |
| Sprache: | Unbestimmt |
| veröffentlicht: |
International Union of Crystallography (IUCr)
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| Schlagwörter: |
| author_facet |
Sasaki, Daisuke Watanabe, Tatiana F. Eady, Robert R. Garratt, Richard C. Antonyuk, Svetlana V. Hasnain, S. Samar Sasaki, Daisuke Watanabe, Tatiana F. Eady, Robert R. Garratt, Richard C. Antonyuk, Svetlana V. Hasnain, S. Samar |
|---|---|
| author |
Sasaki, Daisuke Watanabe, Tatiana F. Eady, Robert R. Garratt, Richard C. Antonyuk, Svetlana V. Hasnain, S. Samar |
| spellingShingle |
Sasaki, Daisuke Watanabe, Tatiana F. Eady, Robert R. Garratt, Richard C. Antonyuk, Svetlana V. Hasnain, S. Samar IUCrJ Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes Condensed Matter Physics General Materials Science Biochemistry General Chemistry |
| author_sort |
sasaki, daisuke |
| spelling |
Sasaki, Daisuke Watanabe, Tatiana F. Eady, Robert R. Garratt, Richard C. Antonyuk, Svetlana V. Hasnain, S. Samar 2052-2525 International Union of Crystallography (IUCr) Condensed Matter Physics General Materials Science Biochemistry General Chemistry http://dx.doi.org/10.1107/s2052252520005230 <jats:p>Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitrogen cycle where nitrate is used in place of dioxygen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the <jats:italic>Hyphomicrobium denitrificans</jats:italic> strain 1NES1 (<jats:italic>Hd</jats:italic> <jats:sub>1NES1</jats:sub>NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system.</jats:p> Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes IUCrJ |
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International Union of Crystallography (IUCr), 2020 |
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International Union of Crystallography (IUCr), 2020 |
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| title |
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_unstemmed |
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_full |
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_fullStr |
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_full_unstemmed |
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_short |
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_sort |
structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| topic |
Condensed Matter Physics General Materials Science Biochemistry General Chemistry |
| url |
http://dx.doi.org/10.1107/s2052252520005230 |
| publishDate |
2020 |
| physical |
557-565 |
| description |
<jats:p>Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitrogen cycle where nitrate is used in place of dioxygen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the <jats:italic>Hyphomicrobium denitrificans</jats:italic> strain 1NES1 (<jats:italic>Hd</jats:italic>
<jats:sub>1NES1</jats:sub>NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system.</jats:p> |
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| author | Sasaki, Daisuke, Watanabe, Tatiana F., Eady, Robert R., Garratt, Richard C., Antonyuk, Svetlana V., Hasnain, S. Samar |
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| description | <jats:p>Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitrogen cycle where nitrate is used in place of dioxygen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the <jats:italic>Hyphomicrobium denitrificans</jats:italic> strain 1NES1 (<jats:italic>Hd</jats:italic> <jats:sub>1NES1</jats:sub>NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system.</jats:p> |
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| spelling | Sasaki, Daisuke Watanabe, Tatiana F. Eady, Robert R. Garratt, Richard C. Antonyuk, Svetlana V. Hasnain, S. Samar 2052-2525 International Union of Crystallography (IUCr) Condensed Matter Physics General Materials Science Biochemistry General Chemistry http://dx.doi.org/10.1107/s2052252520005230 <jats:p>Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitrogen cycle where nitrate is used in place of dioxygen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the <jats:italic>Hyphomicrobium denitrificans</jats:italic> strain 1NES1 (<jats:italic>Hd</jats:italic> <jats:sub>1NES1</jats:sub>NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system.</jats:p> Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes IUCrJ |
| spellingShingle | Sasaki, Daisuke, Watanabe, Tatiana F., Eady, Robert R., Garratt, Richard C., Antonyuk, Svetlana V., Hasnain, S. Samar, IUCrJ, Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes, Condensed Matter Physics, General Materials Science, Biochemistry, General Chemistry |
| title | Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_full | Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_fullStr | Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_full_unstemmed | Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_short | Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_sort | structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| title_unstemmed | Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes |
| topic | Condensed Matter Physics, General Materials Science, Biochemistry, General Chemistry |
| url | http://dx.doi.org/10.1107/s2052252520005230 |