1gjq
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Cyanide binding to fully reduced Pseudomonas aeruginosa cd(1) nitrite | + | Cyanide binding to fully reduced Pseudomonas aeruginosa cd(1) nitrite reductase (Pa cd(1) NiR) has been investigated for the wild-type enzyme and a site-directed mutant in which the active-site His369 was replaced by Ala. This mutation reduces the affinity toward cyanide (by approximately 13-fold) and especially decreases the rate of binding of cyanide to the reduced d(1) heme (by approximately 100-fold). The crystal structure of wild-type reduced Pa cd(1) NiR saturated with cyanide was determined to a resolution of 2.7 A. Cyanide binds to the iron of the d(1) heme, with an Fe-C-N angle of 168 degrees for both subunits of the dimer and only His369 is within hydrogen bonding distance of the nitrogen atom of the ligand. These results suggest that in Pa cd(1) NiR the invariant distal residue His369 plays a dominant role in controlling the binding of anionic ligands and allow the discussion of the mechanism of cyanide binding to the wild-type enzyme. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Transferred entry: 1 | + | [[Category: Transferred entry: 1 7.2 1]] |
[[Category: Brown, K.]] | [[Category: Brown, K.]] | ||
[[Category: Cambillau, C.]] | [[Category: Cambillau, C.]] | ||
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[[Category: reductase]] | [[Category: reductase]] | ||
| - | ''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 12:50:50 2008'' |
Revision as of 10:50, 21 February 2008
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PSEUDOMONAS AERUGINOSA CD1 NITRITE REDUCTASE REDUCED CYANIDE COMPLEX
Overview
Cyanide binding to fully reduced Pseudomonas aeruginosa cd(1) nitrite reductase (Pa cd(1) NiR) has been investigated for the wild-type enzyme and a site-directed mutant in which the active-site His369 was replaced by Ala. This mutation reduces the affinity toward cyanide (by approximately 13-fold) and especially decreases the rate of binding of cyanide to the reduced d(1) heme (by approximately 100-fold). The crystal structure of wild-type reduced Pa cd(1) NiR saturated with cyanide was determined to a resolution of 2.7 A. Cyanide binds to the iron of the d(1) heme, with an Fe-C-N angle of 168 degrees for both subunits of the dimer and only His369 is within hydrogen bonding distance of the nitrogen atom of the ligand. These results suggest that in Pa cd(1) NiR the invariant distal residue His369 plays a dominant role in controlling the binding of anionic ligands and allow the discussion of the mechanism of cyanide binding to the wild-type enzyme.
About this Structure
1GJQ is a Single protein structure of sequence from Pseudomonas aeruginosa with , and as ligands. Active as Transferred entry: 1.7.2.1, with EC number 1.9.3.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Cyanide binding to cd(1) nitrite reductase from Pseudomonas aeruginosa: role of the active-site His369 in ligand stabilization., Sun W, Arese M, Brunori M, Nurizzo D, Brown K, Cambillau C, Tegoni M, Cutruzzola F, Biochem Biophys Res Commun. 2002 Feb 15;291(1):1-7. PMID:11829453
Page seeded by OCA on Thu Feb 21 12:50:50 2008
