7og7: Difference between revisions
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New page: '''Unreleased structure''' The entry 7og7 is ON HOLD Authors: Prasser, B., Schoener, L., Zhang, L., Einsle, O. Description: Crystal structure of the copper chaperone NosL from Shewanel... |
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The | ==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: Prasser | == References == | ||
[[Category: Schoener | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Einsle O]] | |||
[[Category: Prasser B]] | |||
[[Category: Schoener L]] | |||
[[Category: Zhang L]] | |||
Latest revision as of 06:14, 19 June 2024
Crystal structure of the copper chaperone NosL from Shewanella denitrificans
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