6ck1: Difference between revisions
New page: '''Unreleased structure''' The entry 6ck1 is ON HOLD Authors: Yukl, E.T. Description: Crystal structure of Paracoccus denitrificans AztD Category: Unreleased Structures [[Category:... |
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==Crystal structure of Paracoccus denitrificans AztD== | |||
<StructureSection load='6ck1' size='340' side='right'caption='[[6ck1]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ck1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pardp Pardp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CK1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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">Pden_1598 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP])</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=6ck1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ck1 OCA], [http://pdbe.org/6ck1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ck1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ck1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ck1 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Zinc acquisition from limited environments is critical for bacterial survival and pathogenesis. AztD has been identified as a periplasmic or cell surface zinc-binding protein in numerous bacterial species. In Paracoccus denitrificans, AztD can transfer zinc directly to AztC, the solute binding protein for a zinc-specific ATP-binding cassette transporter system, suggesting a role in zinc acquisition and homeostasis. Here, we present the first cry stal structures of AztD from P. denitrificans and tbe human pathogen Citrobacter koseri, revealing a beta-propeller fold and two high-affinity zinc-binding sites that are highly conserved among AztD homologs. These structures combined with transfer assays using WT and mutant proteins provide rare insight into the mechanism of direct zinc transfer from one protein to another. Given the importance of zinc import to bacterial pathogenesis, these insights may prove valuable to the development of zinc transfer inhibitors as antibiotics. | |||
Crystal structures of AztD provide mechanistic insights into direct zinc transfer between proteins.,Neupane DP, Fullam SH, Chacon KN, Yukl ET Commun Biol. 2019 Aug 9;2:308. doi: 10.1038/s42003-019-0542-z. eCollection 2019. PMID:31428696<ref>PMID:31428696</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Yukl, E | <div class="pdbe-citations 6ck1" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pardp]] | |||
[[Category: Yukl, E T]] | |||
[[Category: Beta propeller]] | |||
[[Category: Metal binding protein]] | |||
[[Category: Periplasm]] | |||
[[Category: Zinc]] | |||
Latest revision as of 13:47, 1 January 2020
Crystal structure of Paracoccus denitrificans AztDCrystal structure of Paracoccus denitrificans AztD
Structural highlights
Publication Abstract from PubMedZinc acquisition from limited environments is critical for bacterial survival and pathogenesis. AztD has been identified as a periplasmic or cell surface zinc-binding protein in numerous bacterial species. In Paracoccus denitrificans, AztD can transfer zinc directly to AztC, the solute binding protein for a zinc-specific ATP-binding cassette transporter system, suggesting a role in zinc acquisition and homeostasis. Here, we present the first cry stal structures of AztD from P. denitrificans and tbe human pathogen Citrobacter koseri, revealing a beta-propeller fold and two high-affinity zinc-binding sites that are highly conserved among AztD homologs. These structures combined with transfer assays using WT and mutant proteins provide rare insight into the mechanism of direct zinc transfer from one protein to another. Given the importance of zinc import to bacterial pathogenesis, these insights may prove valuable to the development of zinc transfer inhibitors as antibiotics. Crystal structures of AztD provide mechanistic insights into direct zinc transfer between proteins.,Neupane DP, Fullam SH, Chacon KN, Yukl ET Commun Biol. 2019 Aug 9;2:308. doi: 10.1038/s42003-019-0542-z. eCollection 2019. PMID:31428696[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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