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| | <StructureSection load='1rzq' size='340' side='right'caption='[[1rzq]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1rzq' size='340' side='right'caption='[[1rzq]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rzq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_cycloclastes"_(gray_and_thornton)_bergey_et_al. "achromobacter cycloclastes" (gray and thornton) bergey et al.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RZQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rzq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rzp|1rzp]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzq OCA], [https://pdbe.org/1rzq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rzq RCSB], [https://www.ebi.ac.uk/pdbsum/1rzq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rzq ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzq OCA], [http://pdbe.org/1rzq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rzq RCSB], [http://www.ebi.ac.uk/pdbsum/1rzq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rzq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NIR_ACHCY NIR_ACHCY] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Achromobacter cycloclastes]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: An, X M]] | + | [[Category: An XM]] |
| - | [[Category: Chang, T]] | + | [[Category: Chang T]] |
| - | [[Category: Chang, W C]] | + | [[Category: Chang WC]] |
| - | [[Category: Chang, W R]] | + | [[Category: Chang WR]] |
| - | [[Category: Gall, J Le]] | + | [[Category: Gui LL]] |
| - | [[Category: Gui, L L]] | + | [[Category: Le Gall J]] |
| - | [[Category: Li, H T]] | + | [[Category: Li HT]] |
| - | [[Category: Liu, M Y]] | + | [[Category: Liu MY]] |
| - | [[Category: Wang, C]] | + | [[Category: Wang C]] |
| - | [[Category: Zhang, J P]] | + | [[Category: Zhang JP]] |
| - | [[Category: Denitrification]]
| + | |
| - | [[Category: Greek key beta barrel]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Ph profile]]
| + | |
| - | [[Category: Residue deletion]]
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| Structural highlights
Function
NIR_ACHCY
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li HT, Wang C, Chang T, Chang WC, Liu MY, Le Gall J, Gui LL, Zhang JP, An XM, Chang WR. pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes. Biochem Biophys Res Commun. 2004 Mar 26;316(1):107-13. PMID:15003518 doi:10.1016/j.bbrc.2004.01.177
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