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4ayh

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Revision as of 15:21, 11 August 2016

The X-ray structure of zinc bound ZinT

Structural highlights

4ayh is a 1 chain structure with sequence from "bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4arh, 4aw8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

BACKGROUND: In Gram-negative bacteria the ZnuABC transporter ensures adequate zinc import in Zn(II)-poor environments, like those encountered by pathogens within the infected host. Recently, the metal-binding protein ZinT was suggested to operate as an accessory component of ZnuABC in periplasmic zinc recruitment. Since ZinT is known to form a ZinT-ZnuA complex in the presence of Zn(II) it was proposed to transfer Zn(II) to ZnuA. The present work was undertaken to test this claim. METHODS: ZinT and its structural relationship with ZnuA have been characterized by multiple biophysical techniques (X-ray crystallography, SAXS, analytical ultracentrifugation, fluorescence spectroscopy). RESULTS: The metal-free and metal-bound crystal structures of Salmonella enterica ZinT show one Zn(II) binding site and limited structural changes upon metal removal. Spectroscopic titrations with Zn(II) yield a KD value of 22+/-2nM for ZinT, while those with ZnuA point to one high affinity (KD<20nM) and one low affinity Zn(II) binding site (KD in the micromolar range). Sedimentation velocity experiments established that Zn(II)-bound ZinT interacts with ZnuA, whereas apo-ZinT does not. The model of the ZinT-ZnuA complex derived from small angle X-ray scattering experiments points to a disposition that favors metal transfer as the metal binding cavities of the two proteins face each other. CONCLUSIONS: ZinT acts as a Zn(II)-buffering protein that delivers Zn(II) to ZnuA. GENERAL SIGNIFICANCE: Knowledge of the ZinT-ZnuA relationship is crucial for understanding bacterial Zn(II) uptake.

The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc.,Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E Biochim Biophys Acta. 2014 Jan;1840(1):535-44. doi: 10.1016/j.bbagen.2013.10.010., Epub 2013 Oct 12. PMID:24128931^[1]

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

References

↑ Ilari A, Alaleona F, Tria G, Petrarca P, Battistoni A, Zamparelli C, Verzili D, Falconi M, Chiancone E. The Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zinc. Biochim Biophys Acta. 2014 Jan;1840(1):535-44. doi: 10.1016/j.bbagen.2013.10.010., Epub 2013 Oct 12. PMID:24128931 doi:http://dx.doi.org/10.1016/j.bbagen.2013.10.010

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ayh"

@@ Line 1: / Line 1: @@
 ==The X-ray structure of zinc bound ZinT==
 <StructureSection load='4ayh' size='340' side='right' caption='[[4ayh]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4arh|4arh]], [[4aw8|4aw8]]</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=4ayh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ayh RCSB], [http://www.ebi.ac.uk/pdbsum/4ayh 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=4ayh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayh OCA], [http://pdbe.org/4ayh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ayh RCSB], [http://www.ebi.ac.uk/pdbsum/4ayh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayh ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ayh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ayh

From Proteopedia

Revision as of 15:21, 11 August 2016

The X-ray structure of zinc bound ZinT

Structural highlights

Publication Abstract from PubMed

References

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