1rzq

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{{Seed}}
 
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[[Image:1rzq.png|left|200px]]
 
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==Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0==
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The line below this paragraph, containing "STRUCTURE_1rzq", creates the "Structure Box" on the page.
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<StructureSection load='1rzq' size='340' side='right'caption='[[1rzq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<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>
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{{STRUCTURE_1rzq| PDB=1rzq | SCENE= }}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NIR_ACHCY NIR_ACHCY]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rz/1rzq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rzq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===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:15003518<ref>PMID:15003518</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1rzq" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15003518}}, adds the Publication Abstract to the page
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*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15003518 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15003518}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1RZQ is a 3 chains structure of sequences from [http://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].
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==Reference==
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<ref group="xtra">PMID:15003518</ref><references group="xtra"/>
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[[Category: Achromobacter cycloclastes]]
[[Category: Achromobacter cycloclastes]]
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[[Category: An, X M.]]
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[[Category: Large Structures]]
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[[Category: Chang, T.]]
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[[Category: An XM]]
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[[Category: Chang, W C.]]
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[[Category: Chang T]]
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[[Category: Chang, W R.]]
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[[Category: Chang WC]]
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[[Category: Gall, J Le.]]
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[[Category: Chang WR]]
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[[Category: Gui, L L.]]
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[[Category: Gui LL]]
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[[Category: Li, H T.]]
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[[Category: Le Gall J]]
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[[Category: Liu, M Y.]]
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[[Category: Li HT]]
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[[Category: Wang, C.]]
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[[Category: Liu MY]]
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[[Category: Zhang, J P.]]
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[[Category: Wang C]]
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[[Category: Denitrification]]
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[[Category: Zhang JP]]
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[[Category: Greek key beta barrel]]
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[[Category: Ph profile]]
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[[Category: Residue deletion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:22:58 2009''
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Current revision

Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0

PDB ID 1rzq

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