4u9r
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure of the N-terminal Extension from Cupriavidus metallidurans CzcP== | |
+ | <StructureSection load='4u9r' size='340' side='right'caption='[[4u9r]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4u9r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans_CH34 Cupriavidus metallidurans CH34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U9R 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]] 2.17Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=TCE:3,3,3-PHOSPHANETRIYLTRIPROPANOIC+ACID'>TCE</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=4u9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u9r OCA], [https://pdbe.org/4u9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u9r RCSB], [https://www.ebi.ac.uk/pdbsum/4u9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u9r ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q1LAJ7_CUPMC Q1LAJ7_CUPMC] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The P1B-ATPases, which couple cation transport across membranes to ATP hydrolysis, are central to metal homeostasis in all organisms. An important feature of P1B-ATPases is the presence of soluble metal binding domains (MBDs) that regulate transport activity. Only one type of MBD has been characterized extensively, but bioinformatics analyses indicate that a diversity of MBDs may exist in nature. Here we report the biochemical, structural and functional characterization of a new MBD from the Cupriavidus metallidurans P1B-4-ATPase CzcP (CzcP MBD). The CzcP MBD binds two Cd2+, Co2+ or Zn2+ ions in distinct and unique sites and adopts an unexpected fold consisting of two fused ferredoxin-like domains. Both in vitro and in vivo activity assays using full-length CzcP, truncated CzcP and several variants indicate a regulatory role for the MBD and distinct functions for the two metal binding sites. Taken together, these findings elucidate a previously unknown MBD and suggest new regulatory mechanisms for metal transport by P1B-ATPases. | ||
- | + | A new metal binding domain involved in cadmium, cobalt and zinc transport.,Smith AT, Barupala D, Stemmler TL, Rosenzweig AC Nat Chem Biol. 2015 Jul 20. doi: 10.1038/nchembio.1863. PMID:26192600<ref>PMID:26192600</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 4u9r" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Cupriavidus metallidurans CH34]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Rosenzweig AC]] | ||
+ | [[Category: Smith AT]] |
Current revision
Structure of the N-terminal Extension from Cupriavidus metallidurans CzcP
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