Structural highlights
Publication Abstract from PubMedThe three-dimensional structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with competitive inhibitor glycine has been determined at 2.45 A resolution. It revealed subtle conformational changes providing effective binding of the inhibitor and facilitating labilization of Calpha-protons of the external aldimine. The structure shows that 1, 3-prototropic shift of Calpha-proton to C4'-atom of the cofactor may proceed with participation of active site Lys210 residue whose location is favorable for performing this transformation by a concerted mechanism. The observed stereoselectivity of isotopic exchange of enantiotopic Calpha-protons of glycine may be explained on the basis of external aldimine structure. The exchange of Calpha-pro-(R)-proton of the external aldimine might proceed in the course of the concerted transfer of the proton from Calpha-atom of glycine to C4'-atom of the cofactor. The exchange of Calpha-pro-(S)-proton may be performed with participation of Tyr113 residue which should be present in its basic form. The isotopic exchange of beta-protons, which is observed for amino acids bearing longer side groups, may be effected by two catalytic groups: Lys210 in its basic form, and Tyr113 acting as a general acid. Crystal structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with glycine provides insight in mechanisms of two stages of physiological reaction and isotope exchange of alpha- and beta-protons of competitive inhibitors.,Revtovich SV, Faleev NG, Morozova EA, Anufrieva NV, Nikulin AD, Demidkina TV Biochimie. 2014 Jun;101:161-7. doi: 10.1016/j.biochi.2014.01.007. Epub 2014 Jan, 24. PMID:24463191[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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