2z8p

Structural basis for the catalytic mechanism of phosphothreonine lyase

spinqualitylabelsall models 2z8p, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2z8p is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: PTR, TPO Related: 2z8m, 2z8n, 2z8o 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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