2z8o

From Proteopedia

(Difference between revisions)

Revision as of 13:22, 4 May 2022

Structural basis for the catalytic mechanism of phosphothreonine lyase

Structural highlights

2z8o is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2z8m, 2z8n, 2z8p
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2z8o"

@@ Line 3: / Line 3: @@
 <StructureSection load='2z8o' size='340' side='right'caption='[[2z8o]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<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 [http://proteopedia.org/fgij/fg.htm?mol=2Z8O FirstGlance]. <br>
+<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>
 </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>
 <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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z8m|2z8m]], [[2z8n|2z8n]], [[2z8p|2z8p]]</td></tr>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2z8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z8o OCA], [http://pdbe.org/2z8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2z8o RCSB], [http://www.ebi.ac.uk/pdbsum/2z8o PDBsum], [http://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>
 == 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2z8o

From Proteopedia

Revision as of 13:22, 4 May 2022

Structural basis for the catalytic mechanism of phosphothreonine lyase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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