<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qyu ConSurf].
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Revision as of 13:38, 9 February 2016
Crystal structure of Salmonella effector protein SopA
2qyu is a 1 chain structure with sequence from Salts. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[SOPA_SALTY] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium. Preferentially uses host UBE2D1 (UBCH5A), UBE2D2 (UBCH5B) and UBE2L3 (UBCH7) as E2 ubiquitin-conjugating enzymes.[1][2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Zhang Y, Higashide WM, McCormick BA, Chen J, Zhou D. The inflammation-associated Salmonella SopA is a HECT-like E3 ubiquitin ligase. Mol Microbiol. 2006 Nov;62(3):786-93. PMID:17076670 doi:10.1111/j.1365-2958.2006.05407.x
↑Diao J, Zhang Y, Huibregtse JM, Zhou D, Chen J. Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase. Nat Struct Mol Biol. 2008 Jan;15(1):65-70. Epub 2007 Dec 9. PMID:18066077 doi:10.1038/nsmb1346
↑Diao J, Zhang Y, Huibregtse JM, Zhou D, Chen J. Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase. Nat Struct Mol Biol. 2008 Jan;15(1):65-70. Epub 2007 Dec 9. PMID:18066077 doi:10.1038/nsmb1346
