2g3v

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(New page: 200px<br /><applet load="2g3v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g3v, resolution 2.30&Aring;" /> '''Crystal structure of...)
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[[Image:2g3v.gif|left|200px]]<br /><applet load="2g3v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2g3v, resolution 2.30&Aring;" />
caption="2g3v, resolution 2.30&Aring;" />
'''Crystal structure of CagS (HP0534, Cag13) from Helicobacter pylori'''<br />
'''Crystal structure of CagS (HP0534, Cag13) from Helicobacter pylori'''<br />
==Overview==
==Overview==
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CagZ, a 23 kDa protein encoded by the cagZ gene (HP0526) of the cag, pathogenicity island of Helicobacter pylori, has been cloned, over-expressed, purified and its three-dimensional structure determined., The protein consists of a single compact L-shaped domain, composed of, seven alpha-helices including about 70% of the total residues., Three-dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The, presence of a disordered C-terminal tail and the nature of the molecular, surface suggest that CagZ may participate in the interaction of effector, proteins with one or more components of the H.pylori type IV secretion, system on the cytoplasmic side of the inner membrane.
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CagZ, a 23 kDa protein encoded by the cagZ gene (HP0526) of the cag pathogenicity island of Helicobacter pylori, has been cloned, over-expressed, purified and its three-dimensional structure determined. The protein consists of a single compact L-shaped domain, composed of seven alpha-helices including about 70% of the total residues. Three-dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The presence of a disordered C-terminal tail and the nature of the molecular surface suggest that CagZ may participate in the interaction of effector proteins with one or more components of the H.pylori type IV secretion system on the cytoplasmic side of the inner membrane.
==About this Structure==
==About this Structure==
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2G3V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G3V OCA].
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2G3V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3V OCA].
==Reference==
==Reference==
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[[Category: type iv secretion system]]
[[Category: type iv secretion system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:56 2008''

Revision as of 15:27, 21 February 2008


2g3v, resolution 2.30Å

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Crystal structure of CagS (HP0534, Cag13) from Helicobacter pylori

Overview

CagZ, a 23 kDa protein encoded by the cagZ gene (HP0526) of the cag pathogenicity island of Helicobacter pylori, has been cloned, over-expressed, purified and its three-dimensional structure determined. The protein consists of a single compact L-shaped domain, composed of seven alpha-helices including about 70% of the total residues. Three-dimensional homology searches did not reveal structural homologues, and CagZ can be considered representative of a new protein fold. The presence of a disordered C-terminal tail and the nature of the molecular surface suggest that CagZ may participate in the interaction of effector proteins with one or more components of the H.pylori type IV secretion system on the cytoplasmic side of the inner membrane.

About this Structure

2G3V is a Protein complex structure of sequences from Helicobacter pylori. Full crystallographic information is available from OCA.

Reference

Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system., Cendron L, Seydel A, Angelini A, Battistutta R, Zanotti G, J Mol Biol. 2004 Jul 16;340(4):881-9. PMID:15223328

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