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New page: left|200px<br /><applet load="1jl5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jl5, resolution 2.10Å" /> '''Novel Molecular Arch...
 
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[[Image:1jl5.jpg|left|200px]]<br /><applet load="1jl5" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jl5.jpg|left|200px]]<br /><applet load="1jl5" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jl5, resolution 2.10&Aring;" />
caption="1jl5, resolution 2.10&Aring;" />
'''Novel Molecular Architecture of YopM-a Leucine-rich Effector Protein from Yersinia pestis'''<br />
'''Novel Molecular Architecture of YopM-a Leucine-rich Effector Protein from Yersinia pestis'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
1JL5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JL5 OCA].  
1JL5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL5 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yersinia pestis]]
[[Category: Yersinia pestis]]
[[Category: Anderson, D.E.]]
[[Category: Anderson, D E.]]
[[Category: Evdokimov, A.G.]]
[[Category: Evdokimov, A G.]]
[[Category: Routzahn, K.M.]]
[[Category: Routzahn, K M.]]
[[Category: Waugh, D.S.]]
[[Category: Waugh, D S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: effector protein]]
[[Category: effector protein]]
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[[Category: virulence factor]]
[[Category: virulence factor]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:55 2008''

Revision as of 14:23, 21 February 2008

File:1jl5.jpg


1jl5, resolution 2.10Å

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Novel Molecular Architecture of YopM-a Leucine-rich Effector Protein from Yersinia pestis

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 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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