2ogw

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[[Image:2ogw.jpg|left|200px]]
[[Image:2ogw.jpg|left|200px]]
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{{Structure
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|PDB= 2ogw |SIZE=350|CAPTION= <scene name='initialview01'>2ogw</scene>, resolution 1.83&Aring;
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The line below this paragraph, containing "STRUCTURE_2ogw", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_2ogw| PDB=2ogw | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ogw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ogw OCA], [http://www.ebi.ac.uk/pdbsum/2ogw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ogw RCSB]</span>
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'''Structure of ABC type zinc transporter from E. coli'''
'''Structure of ABC type zinc transporter from E. coli'''
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[[Category: Sharma, A.]]
[[Category: Sharma, A.]]
[[Category: Yogavel, M.]]
[[Category: Yogavel, M.]]
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[[Category: abc]]
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[[Category: Abc]]
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[[Category: transporter]]
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[[Category: Transporter]]
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[[Category: zinc]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:53:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:17:38 2008''
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Revision as of 07:53, 4 May 2008

Image:2ogw.jpg

Template:STRUCTURE 2ogw

Structure of ABC type zinc transporter from E. coli


Overview

ATP-binding cassette superfamily of periplasmic metal transporters are known to be vital for maintaining ion homeostasis in several pathogenic and non-pathogenic bacteria. We have determined crystal structure of the high-affinity zinc transporter ZnuA from Escherichia coli at 1.8 A resolution. This structure represents the first native (non-recombinant) protein structure of a periplasmic metal binding protein. ZnuA reveals numerous conformational features, which occur either in Zn(2+) or in Mn(2+) transporters, and presents a unique conformational state. A comprehensive comparison of ZnuA with other periplasmic ligand binding protein structures suggests vital mechanistic differences between bound and release states of metal transporters. The key new attributes in ZnuA include a C-domain disulfide bond, an extra alpha-helix proximal to the highly charged metal chelating mobile loop region, alternate conformations of secondary shell stabilizing residues at the metal binding site, and domain movements potentially controlled by salt bridges. Based on in-depth structural analyses of five metal binding transporters, we present here a mechanistic model termed as "partial domain slippage" for binding and release of Zn(2+).

About this Structure

2OGW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural analysis of ABC-family periplasmic zinc binding protein provides new insights into mechanism of ligand uptake and release., Chandra BR, Yogavel M, Sharma A, J Mol Biol. 2007 Apr 6;367(4):970-82. Epub 2007 Jan 23. PMID:17306297 Page seeded by OCA on Sun May 4 10:53:29 2008

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