1rzq
From Proteopedia
(New page: 200px<br /><applet load="1rzq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzq, resolution 2.2Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1rzq.jpg|left|200px]]<br /><applet load="1rzq" size=" | + | [[Image:1rzq.jpg|left|200px]]<br /><applet load="1rzq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rzq, resolution 2.2Å" /> | caption="1rzq, resolution 2.2Å" /> | ||
'''Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0'''<br /> | '''Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures of C-terminal despentapeptide nitrite reductase | + | 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== | ==About this Structure== | ||
| - | 1RZQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with CU, SO4 and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http:// | + | 1RZQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nitrite reductase (NO-forming)]] | [[Category: Nitrite reductase (NO-forming)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: An, X | + | [[Category: An, X M.]] |
[[Category: Chang, T.]] | [[Category: Chang, T.]] | ||
| - | [[Category: Chang, W | + | [[Category: Chang, W C.]] |
| - | [[Category: Chang, W | + | [[Category: Chang, W R.]] |
| - | [[Category: Gall, J | + | [[Category: Gall, J Le.]] |
| - | [[Category: Gui, L | + | [[Category: Gui, L L.]] |
| - | [[Category: Li, H | + | [[Category: Li, H T.]] |
| - | [[Category: Liu, M | + | [[Category: Liu, M Y.]] |
[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
| - | [[Category: Zhang, J | + | [[Category: Zhang, J P.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: residue deletion]] | [[Category: residue deletion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:22 2008'' |
Revision as of 12:56, 21 February 2008
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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 with , and as ligands. Active as Nitrite reductase (NO-forming), with EC number 1.7.2.1 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 Thu Feb 21 14:56:22 2008
Categories: Achromobacter cycloclastes | Nitrite reductase (NO-forming) | Single protein | An, X M. | Chang, T. | Chang, W C. | Chang, W R. | Gall, J Le. | Gui, L L. | Li, H T. | Liu, M Y. | Wang, C. | Zhang, J P. | ACY | CU | SO4 | Denitrification | Greek key beta barrel | Ph profile | Residue deletion
