7vw0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of a dimeric periplasmic protein== | |
| + | <StructureSection load='7vw0' size='340' side='right'caption='[[7vw0]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7vw0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VW0 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]] 1.447Å</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=7vw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vw0 OCA], [https://pdbe.org/7vw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vw0 RCSB], [https://www.ebi.ac.uk/pdbsum/7vw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vw0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/V5J1S8_ECOLX V5J1S8_ECOLX] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteria maintain copper balance by various copper response mechanisms. A plasmid gene encoding a methionine rich protein targeted to periplasm is adjacent to the sil operon that confers heavy metal resistance. However, the gene product Orf91 has not been characterized before. Using X-ray crystallography, we solved the structures of Orf91 in apo, cuprous ion-bound, and cupric ion-bound forms. An Orf91 protomer consists of three helices of which the C-terminal two helices belong to domain of unknown function 305 (DUF305), and two Orf91s dimerize into a six-helical bundle. The MxxHH motif specific for DUF305 is critical for cuprous ion binding, and the MxxMxxMHxxMM motif in the N-terminal helix contributes to cupric ion binding. The first histidine of MxxHH shows alternative conformations related to the redox state of copper ion. We suggest that Orf91 is an adaptable copper sponge in the periplasmic space. | ||
| - | + | Structural basis of copper binding by a dimeric periplasmic protein forming a six-helical bundle.,Yang J, Gao M, Wang J, He C, Wang X, Liu L J Inorg Biochem. 2022 Jan 19;229:111728. doi: 10.1016/j.jinorgbio.2022.111728. PMID:35066349<ref>PMID:35066349</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7vw0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liu L]] | ||
| + | [[Category: Yang J]] | ||
Current revision
Structure of a dimeric periplasmic protein
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