6csl
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Pneumococcal PhtD protein 269-339 fragment with bound Zn(II)== | |
+ | <StructureSection load='6csl' size='340' side='right' caption='[[6csl]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6csl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CSL FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6csl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6csl OCA], [http://pdbe.org/6csl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6csl RCSB], [http://www.ebi.ac.uk/pdbsum/6csl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6csl ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The bacterium Streptococcus pneumoniae (the pneumococcus) is a major human pathogen that requires Zn(2+) for its survival and virulence in the host environment. Polyhistidine triad protein D (PhtD) has a known role in pneumococcal Zn(2+) homeostasis. However, the mechanistic basis of PhtD function remains unclear, partly due to a lack of structural information. Here, we determined the crystal structure of the fragment PhtD(269-339) , containing the third Zn(2+) -binding histidine triad (HT) motif of the protein. Analysis of the structure suggests that Zn(2+) -binding occurs at the surface of the protein and that all five HT motifs in the protein bind Zn(2+) and share similar structures. These new structural insights aid in our understanding of how the Pht proteins facilitate pneumococcal Zn(2+) acquisition. This article is protected by copyright. All rights reserved. | ||
- | + | Structural characterisation of the HT3 motif of the polyhistidine triad protein D from Streptococcus pneumoniae.,Luo Z, Pederick VG, Paton JC, McDevitt CA, Kobe B FEBS Lett. 2018 Jun 1. doi: 10.1002/1873-3468.13122. PMID:29856892<ref>PMID:29856892</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6csl" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Kobe, B]] | ||
+ | [[Category: Luo, Z]] | ||
+ | [[Category: McDevitt, C A]] | ||
+ | [[Category: Paton, J C]] | ||
+ | [[Category: Pederick, V G]] | ||
+ | [[Category: Metal binding protein]] | ||
+ | [[Category: Polyhistidine triad]] | ||
+ | [[Category: Zinc homeostasis]] |
Revision as of 07:39, 14 June 2018
Pneumococcal PhtD protein 269-339 fragment with bound Zn(II)
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