1rzq
From Proteopedia
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'''Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0''' | '''Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0''' | ||
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pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes., Li HT, Wang C, Chang T, Chang WC, Liu MY, Le Gall J, Gui LL, Zhang JP, An XM, Chang WR, Biochem Biophys Res Commun. 2004 Mar 26;316(1):107-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15003518 15003518] | pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes., Li HT, Wang C, Chang T, Chang WC, Liu MY, Le Gall J, Gui LL, Zhang JP, An XM, Chang WR, Biochem Biophys Res Commun. 2004 Mar 26;316(1):107-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15003518 15003518] | ||
[[Category: Achromobacter cycloclastes]] | [[Category: Achromobacter cycloclastes]] | ||
| - | [[Category: Nitrite reductase (NO-forming)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: An, X M.]] | [[Category: An, X M.]] | ||
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[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
[[Category: Zhang, J P.]] | [[Category: Zhang, J P.]] | ||
| - | [[Category: | + | [[Category: Denitrification]] |
| - | [[Category: | + | [[Category: Greek key beta barrel]] |
| - | [[Category: | + | [[Category: Ph profile]] |
| - | [[Category: | + | [[Category: Residue deletion]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:06:53 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:06, 3 May 2008
Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0
Overview
Crystal structures of C-terminal despentapeptide nitrite reductase (NiRc-5) from Achromobacter cycloclastes were determined from 1.9 to 2.3A at pH 5.0, 5.4, and 6.2. NiRc-5, that has lost about 30% activity, is found to possess quite similar trimeric structures as the native enzyme. Electron density and copper content measurements indicate that the activity loss is not caused by the release of type 2 copper (T2Cu). pH-profile structural comparisons with native enzyme reveal that the T2Cu active center in NiRc-5 is perturbed, accounting for the partial loss of enzyme activity. This perturbation likely results from the less constrained conformations of two catalytic residues, Asp98 and His255. Hydrogen bonding analysis shows that the deletion of five residues causes a loss of more than half the intersubunit hydrogen bonds mediated by C-terminal tail. This study shows that the C-terminal tail plays an important role in controlling the conformations around the T2Cu site at the subunit interface, and helps keep the optimum microenvironment of active center for the full enzyme activity of AcNiR.
About this Structure
1RZQ is a Single protein structure of sequence from Achromobacter cycloclastes. Full crystallographic information is available from OCA.
Reference
pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes., Li HT, Wang C, Chang T, Chang WC, Liu MY, Le Gall J, Gui LL, Zhang JP, An XM, Chang WR, Biochem Biophys Res Commun. 2004 Mar 26;316(1):107-13. PMID:15003518 Page seeded by OCA on Sat May 3 08:06:53 2008
