4ppv

Crystal Structure of AtCM1 with Phenylalanine Bound in Allosteric Site

spinqualitylabelsall models 4ppv, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ppv is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Ligands: PHE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CM1_ARATH May play a role in chloroplast biogenesis (Potential). Publication Abstract from PubMed Chorismate mutase converts chorismate into prephenate for aromatic amino acid biosynthesis. To understand the molecular basis of allosteric regulation in the plant chorismate mutases, we analyzed the three Arabidopsis thaliana chorismate mutase isoforms (AtCM1-3) and determined the x-ray crystal structures of AtCM1 in complex with phenylalanine and tyrosine. Functional analyses show a wider range of effector control in the Arabidopsis chorismate mutases than previously reported. AtCM1 is activated by tryptophan with phenylalanine and tyrosine acting as negative effectors; however, tryptophan, cysteine, and histidine activate AtCM3. AtCM2 is a nonallosteric form. The crystal structure of AtCM1 in complex with tyrosine and phenylalanine identifies differences in the effector sites of the allosterically regulated yeast enzyme and the other two Arabidopsis isoforms. Site-directed mutagenesis of residues in the effector site reveals key features leading to differential effector regulation in these enzymes. In AtCM1, mutations of Gly-213 abolish allosteric regulation, as observed in AtCM2. A second effector site position, Gly-149 in AtCM1 and Asp-132 in AtCM3, controls amino acid effector specificity in AtCM1 and AtCM3. Comparisons of chorismate mutases from multiple plants suggest that subtle differences in the effector site are conserved in different lineages and may lead to specialized regulation of this branch point enzyme. Structural evolution of differential amino Acid effector regulation in plant chorismate mutases.,Westfall CS, Xu A, Jez JM J Biol Chem. 2014 Oct 10;289(41):28619-28. doi: 10.1074/jbc.M114.591123. Epub, 2014 Aug 26. PMID:25160622 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3D structures of chorismate mutase

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