5i5i

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'''Unreleased structure'''
 
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The entry 5i5i is ON HOLD
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==Shewanella denitrificans nitrous oxide reductase, app form==
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<StructureSection load='5i5i' size='340' side='right'caption='[[5i5i]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5i5i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_denitrificans_OS217 Shewanella denitrificans OS217]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I5I FirstGlance]. <br>
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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]] 2.14&#8491;</td></tr>
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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=5i5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i5i OCA], [https://pdbe.org/5i5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i5i RCSB], [https://www.ebi.ac.uk/pdbsum/5i5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i5i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q12M27_SHEDO Q12M27_SHEDO] Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.[HAMAP-Rule:MF_00716]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The copper enzyme nitrous oxide reductase catalyzes the two-electron reduction of nitrous oxide (N2O) to dinitrogen (N2). Its maturation largely occurs in the periplasm and includes the insertion of at least one Ca2+ ion per monomer. Here we have investigated the role of this structural cation in recombinantly produced apo-N2OR from Shewanella denitrificans and have determined the three-dimensional structure of the protein by X-ray crystallography. In the absence of Ca2+, substantial parts of the enzyme surrounding the binding sites for the copper ions show structural disorder. Reconstitution of the binuclear CuA site was possible in vitro but required the presence of Ca2+ ions for a stable insertion of the center. In contrast, an excess of Ca2+ prevented copper insertion, and the structural analysis of the Ca2+ apo form revealed that the cation is sufficient to structure the disordered regions of the protein even in the absence of Cu ions, indicating that the geometry of the two noncanonical copper centers is largely predetermined by the protein structure.
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Authors: Schneider, L.K., Einsle, O.
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Role of Calcium in Secondary Structure Stabilization during Maturation of Nitrous Oxide Reductase.,Schneider LK, Einsle O Biochemistry. 2016 Feb 29. PMID:26885878<ref>PMID:26885878</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Schneider, L.K]]
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<div class="pdbe-citations 5i5i" style="background-color:#fffaf0;"></div>
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[[Category: Einsle, O]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Shewanella denitrificans OS217]]
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[[Category: Einsle O]]
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[[Category: Schneider LK]]

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Shewanella denitrificans nitrous oxide reductase, app form

PDB ID 5i5i

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