7og7: Difference between revisions
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==Crystal structure of the copper chaperone NosL from Shewanella denitrificans== | ==Crystal structure of the copper chaperone NosL from Shewanella denitrificans== | ||
<StructureSection load='7og7' size='340' side='right'caption='[[7og7]]' scene=''> | <StructureSection load='7og7' size='340' side='right'caption='[[7og7]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == 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> | <table><tr><td colspan='2'>[[7og7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shedo Shedo]. 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='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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Sden_2215 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318161 SHEDO])</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> | </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> | |||
</div> | |||
<div class="pdbe-citations 7og7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Einsle O]] | [[Category: Shedo]] | ||
[[Category: Prasser B]] | [[Category: Einsle, O]] | ||
[[Category: Schoener L]] | [[Category: Prasser, B]] | ||
[[Category: Zhang L]] | [[Category: Schoener, L]] | ||
[[Category: Zhang, L]] | |||
[[Category: Copper chaperone]] | |||
[[Category: Metal binding protein]] | |||
Revision as of 06:23, 18 August 2021
Crystal structure of the copper chaperone NosL from Shewanella denitrificans
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