7tcs

M379A mutant tyrosine phenol-lyase complexed with L-methionine

spinqualitylabelsall models 7tcs, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7tcs is a 4 chain structure with sequence from Citrobacter freundii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.37Å Ligands: CS, DMS, K, PLP, PN9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TPL_CITFR Publication Abstract from PubMed The M379A mutant of Citrobacter freundii tyrosine phenol-lyase (TPL) has been prepared. M379A TPL is a robust catalyst to prepare a number of tyrosines substituted at the 3-position with bulky groups that cannot be made with wild type TPL. The three dimensional structures of M379A TPL complexed with L-methionine and 3-bromo-DL-phenylalanine have been determined by X-ray crystallography. Methionine is bound as a quinonoid complex in a closed active site in 3 of 4 chains of homotetrameric M379A TPL. M379A TPL reacts with L-methionine about 8-fold slower than wild type TPL. The temperature dependence shows that the slower reaction is due to less positive activation entropy. The structure of the M379A TPL complex of 3-bromo-DL-phenylalanine has a quinonoid complex in two subunits, with an open active site conformation. The effects of the M379A mutation on TPL suggest that the mutant enzyme has altered the conformational dynamics of the active site. M379A Mutant Tyrosine Phenol-lyase from Citrobacter freundii Has Altered Conformational Dynamics.,Phillips RS, Jones B, Nash S Chembiochem. 2022 Jul 5;23(13):e202200028. doi: 10.1002/cbic.202200028. Epub 2022, May 24. PMID:35577764 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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