2ogw

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(New page: 200px<br /><applet load="2ogw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ogw, resolution 1.83&Aring;" /> '''Structure of ABC typ...)
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[[Image:2ogw.jpg|left|200px]]<br /><applet load="2ogw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ogw, resolution 1.83&Aring;" />
caption="2ogw, resolution 1.83&Aring;" />
'''Structure of ABC type zinc transporter from E. coli'''<br />
'''Structure of ABC type zinc transporter from E. coli'''<br />
==Overview==
==Overview==
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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+).
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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==
==About this Structure==
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2OGW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OGW OCA].
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2OGW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OGW OCA].
==Reference==
==Reference==
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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 Jan 23;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17306297 17306297]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17306297 17306297]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:10:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:18:22 2008''

Revision as of 16:18, 21 February 2008

Image:2ogw.jpg

2ogw, resolution 1.83Å

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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 with as ligand. 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

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