1jl5
Novel Molecular Architecture of YopM-a Leucine-rich Effector Protein from Yersinia pestis
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OverviewOverview
Many Gram-negative bacterial pathogens employ a contact-dependent (type, III) secretion system to deliver effector proteins into the cytosol of, animal or plant cells. Collectively, these effectors enable the bacteria, to evade the immune response of the infected organism by modulating, host-cell functions. YopM, a member of the leucine-rich repeat protein, superfamily, is an effector produced by the bubonic plague bacterium, Yersinia pestis, that is essential for virulence. Here, we report crystal, structures of YopM at 2.4 and 2.1 A resolution. Among all leucine-rich, repeat family members whose atomic coordinates have been reported, the, repeating unit of YopM has the least canonical secondary structure. In, both crystals, four YopM monomers form a hollow cylinder with an inner, diameter of 35 A. The domain that targets YopM for translocation into, eukaryotic cells adopts a well-ordered, alpha-helical conformation that, packs tightly against the proximal leucine-rich repeat module. A similar, alpha-helical domain can be identified in virulence-associated, leucine-rich repeat proteins produced by Salmonella typhimurium and, Shigella flexneri, and in the conceptual translation products of several, open reading frames in Y. pestis.
About this StructureAbout this Structure
1JL5 is a Single protein structure of sequence from Yersinia pestis with CA as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: a leucine-rich repeat protein with the shortest repeating unit., Evdokimov AG, Anderson DE, Routzahn KM, Waugh DS, J Mol Biol. 2001 Sep 28;312(4):807-21. PMID:11575934
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