4e1t: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e1t]] 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=4E1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1T FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e1t]] 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=4E1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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]] 2.263&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=4e1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1t OCA], [https://pdbe.org/4e1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1t RCSB], [https://www.ebi.ac.uk/pdbsum/4e1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1t 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=4e1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1t OCA], [https://pdbe.org/4e1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1t RCSB], [https://www.ebi.ac.uk/pdbsum/4e1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1t 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Intimins and invasins are virulence factors produced by pathogenic Gram-negative bacteria. They contain C-terminal extracellular passenger domains that are involved in adhesion to host cells and N-terminal beta domains that are embedded in the outer membrane. Here, we identify the domain boundaries of an E. coli intimin beta domain and use this information to solve its structure and the beta domain structure of a Y. pseudotuberculosis invasin. Both beta domain structures crystallized as monomers and reveal that the previous range of residues assigned to the beta domain also includes a protease-resistant domain that is part of the passenger. Additionally, we identify 146 nonredundant representative members of the intimin/invasin family based on the boundaries of the highly conserved intimin and invasin beta domains. We then use this set of sequences along with our structural data to find and map the evolutionarily constrained residues within the beta domain.
 
Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis.,Fairman JW, Dautin N, Wojtowicz D, Liu W, Noinaj N, Barnard TJ, Udho E, Przytycka TM, Cherezov V, Buchanan SK Structure. 2012 May 31. PMID:22658748<ref>PMID:22658748</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4e1t" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 17:50, 14 March 2024

X-ray crystal structure of the transmembrane beta-domain from invasin from Yersinia pseudotuberculosisX-ray crystal structure of the transmembrane beta-domain from invasin from Yersinia pseudotuberculosis

Structural highlights

4e1t 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 2.263Å
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.

4e1t, resolution 2.26Å

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