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| ==Structure of the Salmonella plasmid virulence C protein (SpvC) H106N mutant.== | | ==Structure of the Salmonella plasmid virulence C protein (SpvC) H106N mutant.== |
- | <StructureSection load='4h43' size='340' side='right' caption='[[4h43]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='4h43' size='340' side='right'caption='[[4h43]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4h43]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H43 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4h43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H43 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mkaD, PSLT038, salmonella plasmid virulence (spv), spvC, vsdD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h43 OCA], [https://pdbe.org/4h43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h43 RCSB], [https://www.ebi.ac.uk/pdbsum/4h43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h43 ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4h43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h43 OCA], [http://pdbe.org/4h43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h43 RCSB], [http://www.ebi.ac.uk/pdbsum/4h43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h43 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/SPVC_SALTY SPVC_SALTY]] Secreted effector that irreversibly inactivates host MAP kinases by catalyzing the dephosphorylation of the phosphothreonine residue in the pT-X-pY motif in MAPK2/ERK2, MAPK3/ERK1, and p38, via a beta-elimination reaction leading to a dehydrobutyrine residue. Is also able to remove the phosphate group from phospho-JNK in vitro, but JNK may not be a substrate in vivo. Could help suppress localized proinflammatory responses at infection foci in the spleen and liver, and thereby facilitate bacterial growth.<ref>PMID:17303758</ref> <ref>PMID:18060821</ref> <ref>PMID:18084305</ref> <ref>PMID:18284579</ref> | + | [https://www.uniprot.org/uniprot/SPVC_SALTY SPVC_SALTY] Secreted effector that irreversibly inactivates host MAP kinases by catalyzing the dephosphorylation of the phosphothreonine residue in the pT-X-pY motif in MAPK2/ERK2, MAPK3/ERK1, and p38, via a beta-elimination reaction leading to a dehydrobutyrine residue. Is also able to remove the phosphate group from phospho-JNK in vitro, but JNK may not be a substrate in vivo. Could help suppress localized proinflammatory responses at infection foci in the spleen and liver, and thereby facilitate bacterial growth.<ref>PMID:17303758</ref> <ref>PMID:18060821</ref> <ref>PMID:18084305</ref> <ref>PMID:18284579</ref> |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Salty]] | + | [[Category: Large Structures]] |
- | [[Category: Hengge, A C]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
- | [[Category: Johnson, S J]] | + | [[Category: Hengge AC]] |
- | [[Category: Shenoy, A G]] | + | [[Category: Johnson SJ]] |
- | [[Category: Dephosphorylation]] | + | [[Category: Shenoy AG]] |
- | [[Category: Lyase]]
| + | |
- | [[Category: Phosphothreonine lyase]]
| + | |
| Structural highlights
Function
SPVC_SALTY Secreted effector that irreversibly inactivates host MAP kinases by catalyzing the dephosphorylation of the phosphothreonine residue in the pT-X-pY motif in MAPK2/ERK2, MAPK3/ERK1, and p38, via a beta-elimination reaction leading to a dehydrobutyrine residue. Is also able to remove the phosphate group from phospho-JNK in vitro, but JNK may not be a substrate in vivo. Could help suppress localized proinflammatory responses at infection foci in the spleen and liver, and thereby facilitate bacterial growth.[1] [2] [3] [4]
References
- ↑ Li H, Xu H, Zhou Y, Zhang J, Long C, Li S, Chen S, Zhou JM, Shao F. The phosphothreonine lyase activity of a bacterial type III effector family. Science. 2007 Feb 16;315(5814):1000-3. PMID:17303758 doi:http://dx.doi.org/315/5814/1000
- ↑ Zhu Y, Li H, Long C, Hu L, Xu H, Liu L, Chen S, Wang DC, Shao F. Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Mol Cell. 2007 Dec 14;28(5):899-913. Epub 2007 Nov 29. PMID:18060821 doi:S1097-2765(07)00778-2
- ↑ Chen L, Wang H, Zhang J, Gu L, Huang N, Zhou JM, Chai J. Structural basis for the catalytic mechanism of phosphothreonine lyase. Nat Struct Mol Biol. 2008 Jan;15(1):101-2. Epub 2007 Dec 16. PMID:18084305 doi:10.1038/nsmb1329
- ↑ Mazurkiewicz P, Thomas J, Thompson JA, Liu M, Arbibe L, Sansonetti P, Holden DW. SpvC is a Salmonella effector with phosphothreonine lyase activity on host mitogen-activated protein kinases. Mol Microbiol. 2008 Mar;67(6):1371-83. doi: 10.1111/j.1365-2958.2008.06134.x., Epub 2008 Feb 15. PMID:18284579 doi:http://dx.doi.org/10.1111/j.1365-2958.2008.06134.x
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