7og7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the copper chaperone NosL from Shewanella denitrificans== | |
| + | <StructureSection load='7og7' size='340' side='right'caption='[[7og7]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OG7 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]] 1.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7og7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7og7 OCA], [https://pdbe.org/7og7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7og7 RCSB], [https://www.ebi.ac.uk/pdbsum/7og7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7og7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The final step of denitrification is the reduction of nitrous oxide (N 2 O) to N 2 , mediated by Cu-dependent nitrous oxide reductase (N 2 OR). Its metal centers, Cu A and Cu Z , are assembled through sequential provision of twelve Cu(I) ions by a metallochaperone that forms part of a nos gene cluster encoding the enzyme and its accessory factors. The chaperone is the nosL gene product, an 18 kDa lipoprotein predicted to reside in the outer membrane of Gram-negative bacteria. In order to better understand the assembly of N 2 OR, we have produced NosL from Shewanella denitrificans and determined the structure of the metal-loaded chaperone by X-ray crystallography. The protein assembled a hetero-di-nuclear metal site consisting of Zn(II) and Cu(I), as evidenced by anomalous X-ray scattering. While only Cu(I) is delivered to the enzyme, the stabilizing presence of Zn(II) is essential for the functionality and structural integrity of the chaperone. | ||
| - | + | The Copper Chaperone NosL forms a Heterometal Site for Cu Delivery to Nitrous Oxide Reductase.,Prasser B, Schoner L, Zhang L, Einsle O Angew Chem Int Ed Engl. 2021 Jun 25. doi: 10.1002/anie.202106348. PMID:34171184<ref>PMID:34171184</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7og7" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Einsle O]] | ||
| + | [[Category: Prasser B]] | ||
| + | [[Category: Schoener L]] | ||
| + | [[Category: Zhang L]] | ||
Current revision
Crystal structure of the copper chaperone NosL from Shewanella denitrificans
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