2g3v: Difference between revisions

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<StructureSection load='2g3v' size='340' side='right'caption='[[2g3v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2g3v' size='340' side='right'caption='[[2g3v]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2g3v]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G3V FirstGlance]. <br>
<table><tr><td colspan='2'>[[2g3v]] is a 8 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G3V FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cagS, cag13, HP0534 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g3v OCA], [https://pdbe.org/2g3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g3v RCSB], [https://www.ebi.ac.uk/pdbsum/2g3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g3v ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g3v OCA], [https://pdbe.org/2g3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g3v RCSB], [https://www.ebi.ac.uk/pdbsum/2g3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g3v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAGS_HELPY CAGS_HELPY]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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.
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.


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<ref>PMID:15223328</ref>
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:015223328<ref>PMID:015223328</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43504]]
[[Category: Helicobacter pylori]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Angelini, A]]
[[Category: Angelini A]]
[[Category: Battistutta, R]]
[[Category: Battistutta R]]
[[Category: Cendron, L]]
[[Category: Cendron L]]
[[Category: Montecucco, C]]
[[Category: Montecucco C]]
[[Category: Seydel, A]]
[[Category: Seydel A]]
[[Category: Tasca, E]]
[[Category: Tasca E]]
[[Category: Zanotti, G]]
[[Category: Zanotti G]]
[[Category: Helicobacter pylori]]
[[Category: Pathogenicity island]]
[[Category: Type iv secretion system]]
[[Category: Unknown function]]

Latest revision as of 10:54, 23 October 2024

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

Structural highlights

2g3v is a 8 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAGS_HELPY

Publication Abstract from PubMed

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.

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:015223328[1]

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

References

  1. Cendron L, Seydel A, Angelini A, Battistutta R, Zanotti G. Crystal structure of CagZ, a protein from the Helicobacter pylori pathogenicity island that encodes for a type IV secretion system. J Mol Biol. 2004 Jul 16;340(4):881-9. PMID:15223328 doi:10.1016/j.jmb.2004.05.016

2g3v, resolution 2.30Å

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