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1ogy
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of the respiratory nitrate reductase (NapAB) from | + | The structure of the respiratory nitrate reductase (NapAB) from Rhodobacter sphaeroides, the periplasmic heterodimeric enzyme responsible for the first step in the denitrification process, has been determined at a resolution of 3.2 A. The di-heme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. A total of 57 residues at the N- and C-terminal extremities of NapB adopt an extended conformation, embracing the NapA subunit and largely contributing to the total area of 5,900 A(2) buried in the complex. Complex formation was studied further by measuring the variation of the redox potentials of all the cofactors upon binding. The marked effects observed are interpreted in light of the three-dimensional structure and depict a plasticity that contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
| - | [[Category: Adriano, J | + | [[Category: Adriano, J M.]] |
[[Category: Alric, J.]] | [[Category: Alric, J.]] | ||
[[Category: Arnoux, P.]] | [[Category: Arnoux, P.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:38 2008'' |
Revision as of 12:17, 21 February 2008
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CRYSTAL STRUCTURE OF THE HETERODIMERIC NITRATE REDUCTASE FROM RHODOBACTER SPHAEROIDES
Overview
The structure of the respiratory nitrate reductase (NapAB) from Rhodobacter sphaeroides, the periplasmic heterodimeric enzyme responsible for the first step in the denitrification process, has been determined at a resolution of 3.2 A. The di-heme electron transfer small subunit NapB binds to the large subunit with heme II in close proximity to the [4Fe-4S] cluster of NapA. A total of 57 residues at the N- and C-terminal extremities of NapB adopt an extended conformation, embracing the NapA subunit and largely contributing to the total area of 5,900 A(2) buried in the complex. Complex formation was studied further by measuring the variation of the redox potentials of all the cofactors upon binding. The marked effects observed are interpreted in light of the three-dimensional structure and depict a plasticity that contributes to an efficient electron transfer in the complex from the heme I of NapB to the molybdenum catalytic site of NapA.
About this Structure
1OGY is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , and as ligands. Active as Nitrate reductase, with EC number 1.7.99.4 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase., Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D, Nat Struct Biol. 2003 Nov;10(11):928-34. Epub 2003 Oct 5. PMID:14528294
Page seeded by OCA on Thu Feb 21 14:17:38 2008
Categories: Nitrate reductase | Protein complex | Rhodobacter sphaeroides | Adriano, J M. | Alric, J. | Arnoux, P. | Frangioni, B. | Guigliarelli, B. | Pignol, D. | Sabaty, M. | HEC | MGD | MO | SF4 | Oxidoreductase
