2z8o

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<StructureSection load='2z8o' size='340' side='right'caption='[[2z8o]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2z8o' size='340' side='right'caption='[[2z8o]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2z8o]] is a 2 chain structure. 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>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2z8m|2z8m]], [[2z8n|2z8n]], [[2z8p|2z8p]]</div></td></tr>
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<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>
<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>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2z8o" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chai, J]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Chen, L]]
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[[Category: Chai J]]
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[[Category: Gu, L]]
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[[Category: Chen L]]
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[[Category: Huang, N]]
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[[Category: Gu L]]
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[[Category: Wang, H]]
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[[Category: Huang N]]
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[[Category: Zhou, J M]]
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[[Category: Wang H]]
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[[Category: Distorted beta-strand sheet]]
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[[Category: Zhou JM]]
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[[Category: Lyase]]
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[[Category: Short three-helix bundle]]
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Revision as of 08:38, 7 February 2024

Structural basis for the catalytic mechanism of phosphothreonine lyase

PDB ID 2z8o

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