4MKK

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

Summary for 4MKK

• Entry DOI: 10.2210/pdb4mkk/pdb
• Related: 2RFV 4MKJ
• Descriptor: Methionine gamma-lyase, TRIETHYLENE GLYCOL, SODIUM ION, ... (6 entities in total)
• Functional Keywords: pyridoxal-5'-phosphate, plp-dependent enzyme, aminotransferase class-v, lyase, allicine
• Biological source: Citrobacter freundii
• Total number of polymer chains: 1
• Total formula weight: 43766.96

Authors

Revtovich, S.V.,Nikulin, A.D.,Morozova, E.A.,Zakomirdina, L.N.,Demidkina, T.V. (deposition date: 2013-09-05, release date: 2014-11-12, Last modification date: 2023-12-06)

Primary citation

Morozova, E.A.,Revtovich, S.V.,Anufrieva, N.V.,Kulikova, V.V.,Nikulin, A.D.,Demidkina, T.V.
Alliin is a suicide substrate of Citrobacter freundii methionine gamma-lyase: structural bases of inactivation of the enzyme.
Acta Crystallogr.,Sect.D, 70:3034-3042, 2014

PubMed Abstract: The interaction of Citrobacter freundii methionine γ-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 β-elimination reaction of alliin to form 2-propenethiosulfinate (allicin), pyruvate and ammonia. The β-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 Å 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.

PubMed: 25372692
DOI: 10.1107/S1399004714020938

Experimental method

X-RAY DIFFRACTION (1.45 Å)