4mkk | pdb_00004mkk

Crystal structure of C115A mutant L-methionine gamma-lyase from Citrobacter freundii modified by allicine

spinqualitylabelsall models 4mkk, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mkk is a 1 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 1.45Å Ligands: C1S, CL, K, LLP, NA, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q84AR1_CITFR Publication Abstract from PubMed The interaction of Citrobacter freundii methionine gamma-lyase (MGL) and the mutant form in which Cys115 is replaced by Ala (MGL C115A) with the nonprotein amino acid (2R)-2-amino-3-[(S)-prop-2-enylsulfinyl]propanoic acid (alliin) was investigated. It was found that MGL catalyzes the beta-elimination reaction of alliin to form 2-propenethiosulfinate (allicin), pyruvate and ammonia. The beta-elimination reaction of alliin is followed by the inactivation and modification of SH groups of the wild-type and mutant enzymes. Three-dimensional structures of inactivated wild-type MGL (iMGL wild type) and a C115A mutant form (iMGL C115A) were determined at 1.85 and 1.45 A resolution and allowed the identification of the SH groups that were oxidized by allicin. On this basis, the mechanism of the inactivation of MGL by alliin, a new suicide substrate of MGL, is proposed. Alliin is a suicide substrate of Citrobacter freundii methionine gamma-lyase: structural bases of inactivation of the enzyme.,Morozova EA, Revtovich SV, Anufrieva NV, Kulikova VV, Nikulin AD, Demidkina TV Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):3034-42. doi:, 10.1107/S1399004714020938. Epub 2014 Oct 29. PMID:25372692 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methionine gamma-lyase 3D structures

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