4xyd
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4xyd is ON HOLD until Paper Publication Authors: Crow, A. Description: Structure of the copper-containing nitric oxide reductase from Roseobacter d...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Nitric oxide reductase from Roseobacter denitrificans (RdNOR)== | |
| + | <StructureSection load='4xyd' size='340' side='right'caption='[[4xyd]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xyd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Roseobacter_denitrificans_OCh_114 Roseobacter denitrificans OCh 114]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XYD FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=4xyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xyd OCA], [https://pdbe.org/4xyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xyd RCSB], [https://www.ebi.ac.uk/pdbsum/4xyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xyd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q16A04_ROSDO Q16A04_ROSDO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Membrane-intrinsic nitric oxide reductases (NORs) are key components of bacterial denitrification pathways with a close evolutionary relationship to the cytochrome oxidase (COX) complex found in aerobic respiratory chains. A key distinction between COX and NOR is the identity of the metal directly opposite the heme b3 within the active site. In NOR, this metal is iron (FeB) whereas in COX it is copper (CuB). The purified NOR of Roseobacter denitrificans contains copper and has modest oxidase activity raising the possibility that a COX-like active site might have independently arisen within the context of a NOR-like protein scaffold. Here we present the crystal structure of the Roseobacter denitrificans NorBC complex and anomalous scattering experiments probing the identity of each metal centre. Our results refute the hypothesis that copper occupies the active site and instead reveal a new metal centre in the small subunit not seen in any other NOR or COX. | ||
| - | + | Structure of the membrane-intrinsic nitric oxide reductase from Roseobacter denitrificans.,Crow A, Matsuda Y, Arata H, Oubrie A Biochemistry. 2016 May 17. PMID:27185533<ref>PMID:27185533</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Crow | + | <div class="pdbe-citations 4xyd" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Roseobacter denitrificans OCh 114]] | ||
| + | [[Category: Crow A]] | ||
Current revision
Nitric oxide reductase from Roseobacter denitrificans (RdNOR)
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