2z8o
From Proteopedia
(Difference between revisions)
(9 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:2z8o.jpg|left|200px]] | ||
- | < | + | ==Structural basis for the catalytic mechanism of phosphothreonine lyase== |
- | + | <StructureSection load='2z8o' size='340' side='right'caption='[[2z8o]], [[Resolution|resolution]] 2.40Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2z8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z8O FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></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=2z8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z8o OCA], [https://pdbe.org/2z8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z8o RCSB], [https://www.ebi.ac.uk/pdbsum/2z8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z8o ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [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> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Salmonella SpvC belongs to a new enzyme family designated phosphothreonine lyases that irreversibly inactivate mitogen-activated protein kinases. The crystal structure of SpvC reported here reveals that the two phosphorylated residues in the substrate peptide predominantly mediate its recognition by SpvC. Substrate-induced conformational changes in SpvC sequester the phosphothreonine in a completely solvent-free environment, preventing the hydrolysis of the phosphate group and facilitating the elimination reaction. | ||
- | + | Structural basis for the catalytic mechanism of phosphothreonine lyase.,Chen L, Wang H, Zhang J, Gu L, Huang N, Zhou JM, Chai J Nat Struct Mol Biol. 2008 Jan;15(1):101-2. Epub 2007 Dec 16. PMID:18084305<ref>PMID:18084305</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2z8o" style="background-color:#fffaf0;"></div> | |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: Chai | + | __TOC__ |
- | [[Category: Chen | + | </StructureSection> |
- | [[Category: Gu | + | [[Category: Large Structures]] |
- | [[Category: Huang | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
- | [[Category: Wang | + | [[Category: Chai J]] |
- | [[Category: Zhou | + | [[Category: Chen L]] |
- | + | [[Category: Gu L]] | |
- | + | [[Category: Huang N]] | |
- | + | [[Category: Wang H]] | |
- | + | [[Category: Zhou JM]] |
Current revision
Structural basis for the catalytic mechanism of phosphothreonine lyase
|