4dq9

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dq9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DQ9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dq9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DQ9 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.59&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4dq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dq9 OCA], [https://pdbe.org/4dq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dq9 RCSB], [https://www.ebi.ac.uk/pdbsum/4dq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dq9 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=4dq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dq9 OCA], [https://pdbe.org/4dq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dq9 RCSB], [https://www.ebi.ac.uk/pdbsum/4dq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dq9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GSPH_VIBCH GSPH_VIBCH]] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for secretion of cholera toxin through the outer membrane.
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[https://www.uniprot.org/uniprot/GSPH_VIBCH GSPH_VIBCH] Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins (By similarity). Required for secretion of cholera toxin through the outer membrane.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The type II secretion complex exports folded proteins from the periplasm to the extracellular milieu. It is used by the pathogenic bacterium Vibrio cholerae to export several proteins, including its major virulence factor, cholera toxin. The pseudopilus is an essential component of the type II secretion system and likely acts as a piston to push the folded proteins across the outer membrane through the secretin pore. The pseudopilus is composed of the major pseudopilin, EpsG, and four minor pseudopilins, EpsH, EpsI, EpsJ and EpsK. We determined the x-ray crystal structure of the head domain of EpsH at 1.59A resolution using molecular replacement with the previously reported EpsH structure, 2qv8, as the template. Three additional N-terminal amino acids present in our construct prevent an artifactual conformation of residues 160-166, present in one of the two monomers of the 2qv8 structure. Additional crystal contacts stabilize a long flexible loop comprised of residues 104-135 that is more disordered in the 2qv8 structure but is partially observed in our structure in very different positions for the two EpsH monomers in the asymmetric unit. In one of the conformations the loop is highly extended. Modeling suggests the highly charged loop is capable of contacting EpsG and possibly secreted protein substrates, suggesting a role in specificity of pseudopilus assembly or secretion function.
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The 1.59A resolution structure of the minor pseudopilin EpsH of Vibrio cholerae reveals a long flexible loop.,Raghunathan K, Vago FS, Grindem D, Ball T, Wedemeyer WJ, Bagdasarian M, Arvidson DN Biochim Biophys Acta. 2013 Dec 4;1844(2):406-415. doi:, 10.1016/j.bbapap.2013.11.013. PMID:24316251<ref>PMID:24316251</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4dq9" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Pseudopilin|Pseudopilin]]
*[[Pseudopilin|Pseudopilin]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
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== References ==
 
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<references/>
 
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</StructureSection>
</StructureSection>

Current revision

Crystal structure of the minor pseudopilin EPSH from the type II secretion system of Vibrio cholerae

PDB ID 4dq9

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