1bl9
From Proteopedia
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'''CONFORMATIONAL CHANGES OCCURRING UPON REDUCTION IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA''' | '''CONFORMATIONAL CHANGES OCCURRING UPON REDUCTION IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA''' | ||
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==Reference== | ==Reference== | ||
Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa., Nurizzo D, Cutruzzola F, Arese M, Bourgeois D, Brunori M, Cambillau C, Tegoni M, Biochemistry. 1998 Oct 6;37(40):13987-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9760233 9760233] | Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa., Nurizzo D, Cutruzzola F, Arese M, Bourgeois D, Brunori M, Cambillau C, Tegoni M, Biochemistry. 1998 Oct 6;37(40):13987-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9760233 9760233] | ||
| - | [[Category: Nitrite reductase (NO-forming)]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Nurizzo, D.]] | [[Category: Nurizzo, D.]] | ||
[[Category: Tegoni, M.]] | [[Category: Tegoni, M.]] | ||
| - | [[Category: | + | [[Category: Conformational change]] |
| - | [[Category: | + | [[Category: Denitrification]] |
| - | [[Category: | + | [[Category: Domain swapping]] |
| - | [[Category: | + | [[Category: Electron transport]] |
| - | [[Category: | + | [[Category: Hemoprotein]] |
| - | [[Category: | + | [[Category: Nitrite reductase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: | + | [[Category: Reduction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:39:37 2008'' | |
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Revision as of 08:39, 2 May 2008
CONFORMATIONAL CHANGES OCCURRING UPON REDUCTION IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA
Overview
Nitrite reductase (NiR) from Pseudomonas aeruginosa (EC 1.9.3.2) (NiR-Pa) is a soluble enzyme catalyzing the reduction of nitrite (NO2-) to nitric oxide (NO). The enzyme is a 120 kDa homodimer, in which each monomer carries one c and one d1 heme. The oxidized and reduced forms of NiR from Paracoccus denitrificans GB17 (previously called Thiosphaera pantotropha) (NiR-Pd) have been described [Fulop, V., et al. (1995) Cell 81, 369-377; Williams, P. A., et al. (1997) Nature 389, 406-412], and we recently reported on the structure of oxidized NiR-Pa at 2.15 A [Nurizzo, D., et al. (1997) Structure 5, 1157-1171]. Although the domains carrying the d1 heme are almost identical in both NiR-Pa and NiR-Pd oxidized and reduced structures, the c heme domains show a different pattern of c heme coordination, depending on the species and the redox state. The sixth d1 heme ligand in oxidized NiR-Pd was found to be Tyr25, whereas in NiR-Pa, the homologuous Tyr10 does not interact directly with Fe3+, but via a hydroxide ion. Furthermore, upon reduction, the axial ligand of the c heme of NiR-Pd changes from His17 to Met108. Finally, in the oxidized NiR-Pa structure, the N-terminal stretch of residues (1-29) of one monomer interacts with the other monomer (domain swapping), which does not occur in NiR-Pd. Here the structure of reduced NiR-Pa is described both in the unbound form and with the physiological product, NO, bound at the d1 heme active site. Although both structures are similar to that of reduced NiR-Pd, significant differences with respect to oxidized NiR-Pd were observed in two regions: (i) a loop in the c heme domain (residues 56-62) is shifted 6 A away and (ii) the hydroxide ion, which is the sixth coordination ligand of the heme, is removed upon reduction and NO binding and the Tyr10 side chain rotates away from the position adopted in the oxidized form. The conformational changes observed in NiR-Pa as the result of reduction are less extensive than those occurring in NiR-Pd. Starting with oxidized structures that differ in many respects, the two enzymes converge, yielding reduced conformations which are very similar to each other, which indicates that the conformational changes involved in catalysis are considerably diverse.
About this Structure
1BL9 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa., Nurizzo D, Cutruzzola F, Arese M, Bourgeois D, Brunori M, Cambillau C, Tegoni M, Biochemistry. 1998 Oct 6;37(40):13987-96. PMID:9760233 Page seeded by OCA on Fri May 2 11:39:37 2008
