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==Crystal structure of ZntB cytoplasmic domain from Vibrio parahaemolyticus RIMD 2210633== | |||
<StructureSection load='3ck6' size='340' side='right'caption='[[3ck6]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ck6]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibpa Vibpa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3bhc 3bhc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CK6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VP2389, NP_798768.1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=223926 VIBPA])</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=3ck6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ck6 OCA], [https://pdbe.org/3ck6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ck6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ck6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ck6 ProSAT], [https://www.topsan.org/Proteins/MCSG/3ck6 TOPSAN]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/3ck6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ck6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ZntB is the distant homolog of CorA Mg(2+) transporter within the metal ion transporter superfamily. It was early reported that the ZntB from Salmonella typhimurium facilitated efflux of Zn(2+) and Cd(2+), but not Mg(2+). Here, we report the 1.90 A crystal structure of the intracellular domain of ZntB from Vibrio parahemolyticus. The domain forms a funnel-shaped homopentamer that is similar to the full-length CorA from Thermatoga maritima, but differs from two previously reported dimeric structures of truncated CorA intracellular domains. However, no Zn(2+) or Cd(2+) binding sites were identified in the high-resolution structure. Instead, 25 well-defined Cl(-) ions were observed and some of these binding sites are highly conserved within the ZntB family. Continuum electrostatics calculations suggest that the central pore of the funnel is highly attractive for cations, especially divalents. The presence of the bound Cl(-) ions increases the stability of cations along the pore suggesting they could be important in enhancing cation transport. | |||
Structure and electrostatic property of cytoplasmic domain of ZntB transporter.,Tan K, Sather A, Robertson JL, Moy S, Roux B, Joachimiak A Protein Sci. 2009 Oct;18(10):2043-52. PMID:19653298<ref>PMID:19653298</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ck6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Joachimiak, A | [[Category: Vibpa]] | ||
[[Category: | [[Category: Joachimiak, A]] | ||
[[Category: Moy, S | [[Category: Structural genomic]] | ||
[[Category: Sather, A | [[Category: Moy, S]] | ||
[[Category: Tan, K | [[Category: Sather, A]] | ||
[[Category: Tan, K]] | |||
[[Category: Apc91421 1]] | [[Category: Apc91421 1]] | ||
[[Category: Cytoplasmic domain]] | [[Category: Cytoplasmic domain]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
[[Category: | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
[[Category: Vibrio parahaemolyticus rimd 2210633]] | [[Category: Vibrio parahaemolyticus rimd 2210633]] | ||
[[Category: Zntb]] | [[Category: Zntb]] | ||
Latest revision as of 22:10, 20 October 2021
Crystal structure of ZntB cytoplasmic domain from Vibrio parahaemolyticus RIMD 2210633Crystal structure of ZntB cytoplasmic domain from Vibrio parahaemolyticus RIMD 2210633
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedZntB is the distant homolog of CorA Mg(2+) transporter within the metal ion transporter superfamily. It was early reported that the ZntB from Salmonella typhimurium facilitated efflux of Zn(2+) and Cd(2+), but not Mg(2+). Here, we report the 1.90 A crystal structure of the intracellular domain of ZntB from Vibrio parahemolyticus. The domain forms a funnel-shaped homopentamer that is similar to the full-length CorA from Thermatoga maritima, but differs from two previously reported dimeric structures of truncated CorA intracellular domains. However, no Zn(2+) or Cd(2+) binding sites were identified in the high-resolution structure. Instead, 25 well-defined Cl(-) ions were observed and some of these binding sites are highly conserved within the ZntB family. Continuum electrostatics calculations suggest that the central pore of the funnel is highly attractive for cations, especially divalents. The presence of the bound Cl(-) ions increases the stability of cations along the pore suggesting they could be important in enhancing cation transport. Structure and electrostatic property of cytoplasmic domain of ZntB transporter.,Tan K, Sather A, Robertson JL, Moy S, Roux B, Joachimiak A Protein Sci. 2009 Oct;18(10):2043-52. PMID:19653298[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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