View source for 3ncw


==Crystal structure of EHEC O157:H7 intimin==
<StructureSection load='3ncw' size='340' side='right'caption='[[3ncw]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ncw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._TW14359 Escherichia coli O157:H7 str. TW14359]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NCW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NCW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=3ncw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ncw OCA], [https://pdbe.org/3ncw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ncw RCSB], [https://www.ebi.ac.uk/pdbsum/3ncw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ncw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EAE_ECO57 EAE_ECO57] Necessary for the production of attaching and effacing lesions on tissue culture cells.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enterohaemorrhagic E. coli (EHEC) O157:H7 is a primary food-borne bacterial pathogen capable of causing life-threatening human infections which poses a serious challenge to public health worldwide. Intimin, the bacterial outer-membrane protein, plays a key role in the initiating process of EHEC infection. This activity is dependent upon translocation of the intimin receptor (Tir), the intimin binding partner of the bacteria-encoded host cell surface protein. Intimin has attracted considerable attention due to its potential function as an antibacterial drug target. Here, we report the crystal structure of the Tir-binding domain of intimin (Int188) from E. coli O157:H7 at 2.8 A resolution, together with a mutant (IntN916Y) at 2.6 A. We also built the structural model of EHEC intimin-Tir complex and analyzed the key binding residues. It suggested that the binding pattern of intimin and Tir between EHEC and Enteropathogenic E. coli (EPEC) adopt a similar mode and they can complement with each other. Detailed structural comparison indicates that there are four major points of structural variations between EHEC and EPEC intimins: one in Domain I (Ig-like domain), the other three located in Domain II (C-type lectin-like domain). These variations result in different binding affinities. These findings provide structural insight into the binding pattern of intimin to Tir and the molecular mechanism of EHEC O157: H7.

Crystal structure of EHEC intimin: insights into the complementarity between EPEC and EHEC.,Yi Y, Ma Y, Gao F, Mao X, Peng H, Feng Y, Fan Z, Wang G, Guo G, Yan J, Zeng H, Zou Q, Gao GF PLoS One. 2010 Dec 16;5(12):e15285. PMID:21179574<ref>PMID:21179574</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ncw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli O157:H7 str. TW14359]]
[[Category: Large Structures]]
[[Category: Gao F]]
[[Category: Gao GF]]
[[Category: Yi Y]]
[[Category: Zou QM]]