1GC2

CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA

Summary for 1GC2

• Entry DOI: 10.2210/pdb1gc2/pdb
• Related: 1GC0
• Descriptor: METHIONINE GAMMA-LYASE (2 entities in total)
• Functional Keywords: pyridoxal-5'-phosphate, lyase
• Biological source: Pseudomonas putida
• Total number of polymer chains: 4
• Total formula weight: 171606.94

Authors

Motoshima, H.,Inagaki, K.,Kumasaka, T.,Furuichi, M.,Inoue, H.,Tamura, T.,Esaki, N.,Soda, K.,Tanaka, N.,Yamamoto, M.,Tanaka, H. (deposition date: 2000-07-06, release date: 2002-05-08, Last modification date: 2023-12-27)

Primary citation

Motoshima, H.,Inagaki, K.,Kumasaka, T.,Furuichi, M.,Inoue, H.,Tamura, T.,Esaki, N.,Soda, K.,Tanaka, N.,Yamamoto, M.,Tanaka, H.
Crystal structure of the pyridoxal 5'-phosphate dependent L-methionine gamma-lyase from Pseudomonas putida.
J.Biochem., 128:349-354, 2000

PubMed Abstract: L-Methionine gamma-lyase (MGL) catalyzes the pyridoxal 5'-phosphate (PLP) dependent alpha,gamma-elimination of L-methionine. We have determined two crystal structures of MGL from Pseudomonas putida using MAD (multiwavelength anomalous diffraction) and molecular replacement methods. The structures have been refined to an R-factor of 21.1% at 2.0 and 1.7 A resolution using synchrotron radiation diffraction data. A homotetramer with 222 symmetry is built up by non-crystallographic symmetry. Two monomers associate to build the active dimer. The spatial fold of subunits, with three functionally distinct domains and their quarternary arrangement, is similar to those of L-cystathionine beta-lyase and L-cystathionine gamma-synthase from Escherichia coli.

PubMed: 10965031
DOI: 10.1093/oxfordjournals.jbchem.a022760

Experimental method

X-RAY DIFFRACTION (2 Å)