2qza: Difference between revisions

Revision as of 19:43, 21 February 2008

Crystal structure of Salmonella effector protein SopA

OverviewOverview

Bacterial pathogens deliver virulence proteins into host cells to facilitate entry and survival. Salmonella SopA functions as an E3 ligase to manipulate the host proinflammatory response. Here we report the crystal structure of SopA in two conformations. Although it has little sequence similarity to eukaryotic HECT-domain E3s, the C-terminal half of SopA has a bilobal architecture that is reminiscent of the N- and C-lobe arrangement of HECT domains. The SopA structure also contains a putative substrate-binding domain located near the E2-binding site. The two structures of SopA differ in the relative orientations of the C lobe, indicating that SopA possesses the conformational flexibility essential for HECT E3 function. These results suggest that SopA is a unique HECT E3 ligase evolved from the coevolutionary selective pressure at the bacterium-host interface.

About this StructureAbout this Structure

2QZA is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase., Diao J, Zhang Y, Huibregtse JM, Zhou D, Chen J, Nat Struct Mol Biol. 2008 Jan;15(1):65-70. Epub 2007 Dec 9. PMID:18066077

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OCA

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 ==Overview==
-Bacterial pathogens deliver virulence proteins into host cells to, facilitate entry and survival. Salmonella SopA functions as an E3 ligase, to manipulate the host proinflammatory response. Here we report the, crystal structure of SopA in two conformations. Although it has little, sequence similarity to eukaryotic HECT-domain E3s, the C-terminal half of, SopA has a bilobal architecture that is reminiscent of the N- and C-lobe, arrangement of HECT domains. The SopA structure also contains a putative, substrate-binding domain located near the E2-binding site. The two, structures of SopA differ in the relative orientations of the C lobe, indicating that SopA possesses the conformational flexibility essential, for HECT E3 function. These results suggest that SopA is a unique HECT E3, ligase evolved from the coevolutionary selective pressure at the, bacterium-host interface.
+Bacterial pathogens deliver virulence proteins into host cells to facilitate entry and survival. Salmonella SopA functions as an E3 ligase to manipulate the host proinflammatory response. Here we report the crystal structure of SopA in two conformations. Although it has little sequence similarity to eukaryotic HECT-domain E3s, the C-terminal half of SopA has a bilobal architecture that is reminiscent of the N- and C-lobe arrangement of HECT domains. The SopA structure also contains a putative substrate-binding domain located near the E2-binding site. The two structures of SopA differ in the relative orientations of the C lobe, indicating that SopA possesses the conformational flexibility essential for HECT E3 function. These results suggest that SopA is a unique HECT E3 ligase evolved from the coevolutionary selective pressure at the bacterium-host interface.
 ==About this Structure==
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 [[Category: ubiquitin e3 ligase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:03:53 2008''
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