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5aq6

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Revision as of 07:43, 3 July 2019

Structure of E. coli ZinT at 1.79 Angstrom

Structural highlights

5aq6 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ZINT_ECOLI] May function as a periplasmic zinc chaperone or mediate direct transport of zinc from the periplasm to the cytoplasm under zinc-limited conditions. Binds zinc with high affinity, and can also bind cadmium, mercury or nickel. Preferentially binds Zn(2+) over Cd(2+). Contains one high affinity metal binding site, and can bind additional metal ions at other sites.^[1] ^[2]

Publication Abstract from PubMed

Escherichia coli ZinT is a metal binding protein involved in zinc homeostasis, with additional putative functions in the resistance against other metals. Herein, a method was designed and implemented to evaluate from a structural and functional viewpoint metal binding to E. coli ZinT in 96-well microtiter plates. The isolated ZinT was mixed with several metal ions and their binding ability was determined by differential scanning fluorimetry. From the positive hits, six metal ions were evaluated in terms of their toxicity towards an E. coli strain depleted of ZinT (DeltazinT) using as control a strain deleted in the galT gene (DeltagalT). The different sensitivities of each strain to the tested metals revealed novel roles of ZinT in the resistance to cobalt, cadmium and mercury. This approach provides a valuable and reliable platform for the analysis of metal binding and its functional implications, extendable to other metal binding proteins. In combination with the developed platform, structural studies were performed with ZinT, with the zinc-loaded crystallographic structure being obtained at 1.79 A resolution. Besides the canonical zinc-binding site located near the N-terminus, the herein reported dimeric ZinT structure unravelled extra zinc binding sites that support its role in metal loading and/or transport. Altogether, the designed experimental platform allowed revealing new roles for the ZinT protein in microbial resistance to heavy metal toxicity, as well as structural insights into the ZinT metal binding mechanism.

Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism.,Colaco HG, Santo PE, Matias PM, Bandeiras TM, Vicente JB Metallomics. 2016 Jan 13. PMID:26758285^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kershaw CJ, Brown NL, Hobman JL. Zinc dependence of zinT (yodA) mutants and binding of zinc, cadmium and mercury by ZinT. Biochem Biophys Res Commun. 2007 Dec 7;364(1):66-71. Epub 2007 Oct 2. PMID:17931600 doi:http://dx.doi.org/10.1016/j.bbrc.2007.09.094
↑ Graham AI, Hunt S, Stokes SL, Bramall N, Bunch J, Cox AG, McLeod CW, Poole RK. Severe zinc depletion of Escherichia coli: roles for high affinity zinc binding by ZinT, zinc transport and zinc-independent proteins. J Biol Chem. 2009 Jul 3;284(27):18377-89. doi: 10.1074/jbc.M109.001503. Epub 2009, Apr 19. PMID:19377097 doi:http://dx.doi.org/10.1074/jbc.M109.001503
↑ Colaco HG, Santo PE, Matias PM, Bandeiras TM, Vicente JB. Roles of Escherichia coli ZinT in cobalt, mercury and cadmium resistance and structural insights into the metal binding mechanism. Metallomics. 2016 Jan 13. PMID:26758285 doi:http://dx.doi.org/10.1039/c5mt00291e

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5aq6"

@@ Line 1: / Line 1: @@
 ==Structure of E. coli ZinT at 1.79 Angstrom==
-<StructureSection load='5aq6' size='340' side='right' caption='[[5aq6]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
+<StructureSection load='5aq6' size='340' side='right'caption='[[5aq6]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5aq6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AQ6 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <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=5aq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aq6 OCA], [http://pdbe.org/5aq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aq6 RCSB], [http://www.ebi.ac.uk/pdbsum/5aq6 PDBsum]</span></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=5aq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aq6 OCA], [http://pdbe.org/5aq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aq6 RCSB], [http://www.ebi.ac.uk/pdbsum/5aq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aq6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 23: / Line 23: @@
 </StructureSection>
 [[Category: Escherichia coli]]
+[[Category: Large Structures]]
 [[Category: Bandeiras, T M]]
 [[Category: Colaco, H G]]

5aq6

From Proteopedia

Revision as of 07:43, 3 July 2019

Structure of E. coli ZinT at 1.79 Angstrom

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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