1cwv: Difference between revisions

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<StructureSection load='1cwv' size='340' side='right'caption='[[1cwv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1cwv' size='340' side='right'caption='[[1cwv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cwv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pseudotuberkulosis"_(sic)_pfeiffer_1889 "bacillus pseudotuberkulosis" (sic) pfeiffer 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CWV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cwv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CWV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=1cwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwv OCA], [https://pdbe.org/1cwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cwv RCSB], [https://www.ebi.ac.uk/pdbsum/1cwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwv 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=1cwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwv OCA], [https://pdbe.org/1cwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cwv RCSB], [https://www.ebi.ac.uk/pdbsum/1cwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/INVA_YERPS INVA_YERPS]] Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins.  
[https://www.uniprot.org/uniprot/INVA_YERPS INVA_YERPS] Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cwv ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cwv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrates such as fibronectin. The 2.3 angstrom crystal structure of the invasin extracellular region reveals five domains that form a 180 angstrom rod with structural similarities to tandem fibronectin type III domains. The integrin-binding surfaces of invasin and fibronectin include similarly located key residues, but in the context of different folds and surface shapes. The structures of invasin and fibronectin provide an example of convergent evolution, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.
Crystal structure of invasin: a bacterial integrin-binding protein.,Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ Science. 1999 Oct 8;286(5438):291-5. PMID:10514372<ref>PMID:10514372</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1cwv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bjorkman, P J]]
[[Category: Yersinia pseudotuberculosis]]
[[Category: Hamburger, Z A]]
[[Category: Bjorkman PJ]]
[[Category: Integrin-binding protein]]
[[Category: Hamburger ZA]]
[[Category: Inv gene]]
[[Category: Structural protein]]

Latest revision as of 18:44, 13 March 2024

CRYSTAL STRUCTURE OF INVASIN: A BACTERIAL INTEGRIN-BINDING PROTEINCRYSTAL STRUCTURE OF INVASIN: A BACTERIAL INTEGRIN-BINDING PROTEIN

Structural highlights

1cwv is a 1 chain structure with sequence from Yersinia pseudotuberculosis. 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

INVA_YERPS Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1cwv, resolution 2.30Å

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