2qyu
From Proteopedia
(New page: 200px<br /><applet load="2qyu" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qyu, resolution 2.10Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Bacterial pathogens deliver virulence proteins into host cells to | + | 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== | ==About this Structure== | ||
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[[Category: ubiquitin e3 ligase]] | [[Category: ubiquitin e3 ligase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:23 2008'' |
Revision as of 16:43, 21 February 2008
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Crystal structure of Salmonella effector protein SopA
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.
About this Structure
2QYU is a Single protein structure of sequence from Salmonella typhimurium with and as ligands. Full crystallographic information is available from OCA.
Reference
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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