View source for 4lgi


==N-terminal truncated NleC structure==
<StructureSection load='4lgi' size='340' side='right'caption='[[4lgi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lgi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LGI FirstGlance]. <br>
</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=4lgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lgi OCA], [https://pdbe.org/4lgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lgi RCSB], [https://www.ebi.ac.uk/pdbsum/4lgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lgi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8X834_ECO57 Q8X834_ECO57] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
NleC is one of the virulence factors that is injected into infected host cells by enteropathogenic and enterohaemorrhagic Escherichia coli (EPEC and EHEC) via a needle-like protein complex called the type III secretion system (T3SS). The cytosolic NleC specifically cleaves the p65 subunit of NF-kappaB in the p65-p50 heterodimeric complex just after the Cys38 site in its N-terminal domain. The degradation of the remainder of the p65 C-terminal domain by the proteasome disrupts the NF-kappaB signalling pathway, thus dampening the host inflammatory response. Here, the crystal structure of NleC is reported at 1.55 A resolution. In conjunction with biochemical analyses, the structure reveals that NleC is a member of the zincin zinc protease family and that the configuration of the NleC active site resembles that of the metzincin clan of metallopeptidases but without the canonical Met turn of astacin. The extended zinc-binding motif of NleC (HEXXHXXTXXXD) includes three metal ligands. The fifth zinc ligand, a conserved tyrosine (a bound water molecule is the fourth ligand), lies 45 residues downstream of the zincin motif. Furthermore, the electrostatic potential complementarity between NleC and p65 also contributes to the cleavage activity of the protease. These results not only provide important insights into the mechanism of how NleC recognizes its substrates, but also shed light on the design of new antibiotics for the food-borne diseases arising from EPEC and EHEC.

Structure and mechanism of a type III secretion protease, NleC.,Li W, Liu Y, Sheng X, Yin P, Hu F, Liu Y, Chen C, Li Q, Yan C, Wang J Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):40-7. doi:, 10.1107/S1399004713024619. Epub 2013 Dec 24. PMID:24419377<ref>PMID:24419377</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lgi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Li WQ]]
[[Category: Liu YX]]
[[Category: Sheng XL]]
[[Category: Wang JW]]
[[Category: Yan CY]]