5M3Z

Crystal structure of Citrobacter freundii methionine gamma-lyase with C115H replacement in the complex with L-norleucine

Summary for 5M3Z

• Entry DOI: 10.2210/pdb5m3z/pdb
• Descriptor: Methionine gamma-lyase, PYRIDOXAL-5'-PHOSPHATE, NORLEUCINE, ... (6 entities in total)
• Functional Keywords: methionine gamma-lyase, c115h substitution, l-norleucine, lyase
• Biological source: Citrobacter freundii
• Total number of polymer chains: 1
• Total formula weight: 43878.61

Authors

Revtovich, S.V.,Nikulin, A.D.,Anufrieva, N.V.,Morozova, E.A.,Demidkina, T.V. (deposition date: 2016-10-17, release date: 2017-06-28, Last modification date: 2024-01-17)

Primary citation

Revtovich, S.V.,Morozova, E.A.,Kulikova, V.V.,Anufrieva, N.V.,Osipova, T.I.,Koval, V.S.,Nikulin, A.D.,Demidkina, T.V.
Crystal structure of mutant form Cys115His of Citrobacter freundii methionine gamma-lyase complexed with l-norleucine.
Biochim. Biophys. Acta, 1865:1123-1128, 2017

PubMed Abstract: The mutant form of Citrobacter freundii methionine γ-lyase with the replacement of active site Cys115 for His has been found to be inactive in the γ-elimination reaction of methionine while fully active in the γ-elimination reaction of O-acetyl-l-homoserine and in the β-elimination reaction of S-alk(en)yl-substituted cysteines. In this work, the crystal structure of the mutant enzyme complexed with competitive inhibitor, l-norleucine was determined at 1.45Å resolution. At the enzyme active site the inhibitor proved to be bound both noncovalently and covalently, which corresponds to the two intermediates of the γ- and β-elimination reactions, Michaelis complex and the external aldimine. Analysis of the structure allowed us to suggest the possible reason for the inability of the mutant enzyme to catalyze the physiological reaction.

PubMed: 28602917
DOI: 10.1016/j.bbapap.2017.06.001

Experimental method

X-RAY DIFFRACTION (1.45 Å)