2RFV

High resolution structure of L-methionine gamma-lyase from Citrobacter freundii

Summary for 2RFV

• Entry DOI: 10.2210/pdb2rfv/pdb
• Related: 1Y4I
• Descriptor: Methionine gamma-lyase, CHLORIDE ION (3 entities in total)
• Functional Keywords: pyridoxal-5'-phosphate, plp-dependent enzyme, lyase
• Biological source: Citrobacter freundii
• Total number of polymer chains: 1
• Total formula weight: 43286.49

Authors

Nikulin, A.D.,Revtovich, S.V.,Morozova, E.A.,Nevskaya, N.A.,Nikonov, S.V.,Garber, M.B.,Demidkina, T.V. (deposition date: 2007-10-02, release date: 2008-08-19, Last modification date: 2023-11-15)

Primary citation

Nikulin, A.,Revtovich, S.,Morozova, E.,Nevskaya, N.,Nikonov, S.,Garber, M.,Demidkina, T.
High-resolution structure of methionine gamma-lyase from Citrobacter freundii.
Acta Crystallogr.,Sect.D, 64:211-218, 2008

PubMed Abstract: Pyridoxal 5'-phosphate-dependent methionine gamma-lyase (MGL) is involved in the metabolism of sulfur-containing amino acids. The enzyme is a promising target in some anaerobic pathogens and is effective in cancer-cell treatment. The structure of the MGL holoenzyme from Citrobacter freundii has previously been determined at 1.9 A resolution. By modification of the crystallization procedure, the previously determined structure of C. freundii MGL has been improved to 1.35 A resolution with R and R(free) values of 0.152 and 0.177, respectively. This high-resolution structure makes it possible to analyze the interactions between the monomers in detail and to reveal the structurally invariant regions that are responsible for monomer-monomer recognition during the formation of the active enzyme. Details of the mode of cofactor binding and of the flexible regions that may be involved in substrate recognition and binding are also described.

PubMed: 18219122
DOI: 10.1107/S0907444907065390

Experimental method

X-RAY DIFFRACTION (1.355 Å)