8gar

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'''Unreleased structure'''
 
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The entry 8gar is ON HOLD until Paper Publication
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==Nitrosomonas europaea Cytochrome P460 Arg44Ala==
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<StructureSection load='8gar' size='340' side='right'caption='[[8gar]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8gar]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GAR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GAR 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]] 1.55&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></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=8gar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gar OCA], [https://pdbe.org/8gar PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gar RCSB], [https://www.ebi.ac.uk/pdbsum/8gar PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gar ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q50927_NITER Q50927_NITER]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cytochrome P460s are heme enzymes that oxidize hydroxylamine to nitrous oxide. They bear specialized "heme P460" cofactors that are cross-linked to their host polypeptides by a post-translationally modified lysine residue. Wild-type N. europaea cytochrome P460 may be isolated as a cross-link-deficient proenzyme following anaerobic overexpression in E. coli. When treated with peroxide, this proenzyme undergoes maturation to active enzyme with spectroscopic and catalytic properties that match wild-type cyt P460. This maturation reactivity requires no chaperones horizontal line it is intrinsic to the protein. This behavior extends to the broader cytochrome c'(beta) superfamily. Accumulated data reveal key contributions from the secondary coordination sphere that enable selective, complete maturation. Spectroscopic data support the intermediacy of a ferryl species along the maturation pathway.
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Authors:
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Cytochrome P460 Cofactor Maturation Proceeds via Peroxide-Dependent Post-translational Modification.,Bollmeyer MM, Coleman RE, Majer SH, Ferrao SD, Lancaster KM J Am Chem Soc. 2023 Jun 20. doi: 10.1021/jacs.3c03608. PMID:37338957<ref>PMID:37338957</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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<div class="pdbe-citations 8gar" style="background-color:#fffaf0;"></div>
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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: Nitrosomonas europaea]]
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[[Category: Bollmeyer MM]]
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[[Category: Lancaster KM]]

Revision as of 05:45, 5 July 2023

Nitrosomonas europaea Cytochrome P460 Arg44Ala

PDB ID 8gar

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