4U1T

The crystal structure of holo CalE6, a methionine gamma lyase from Micromonospora echinospora

Summary for 4U1T

• Entry DOI: 10.2210/pdb4u1t/pdb
• Related: 4U2H
• Descriptor: CalE6, SULFATE ION (3 entities in total)
• Functional Keywords: lyase
• Biological source: Micromonospora echinospora
• Total number of polymer chains: 8
• Total formula weight: 336619.19

Authors

Song, H.G.,Guo, Z.H. (deposition date: 2014-07-16, release date: 2015-01-07, Last modification date: 2023-11-15)

Primary citation

Song, H.,Xu, R.,Guo, Z.
Identification and Characterization of a Methionine gamma-Lyase in the Calicheamicin Biosynthetic Cluster of Micromonospora echinospora
Chembiochem, 16:100-109, 2015

PubMed Abstract: CalE6 is a previously uncharacterized protein involved in the biosynthesis of calicheamicins in Micromonospora echinospora. It is a pyridoxal-5'-phosphate-dependent enzyme and exhibits high sequence homology to cystathionine γ-lyases and cystathionine γ-synthases. However, it was found to be active towards methionine and to convert this amino acid into α-ketobutyrate, ammonium, and methanethiol. The crystal structure of the cofactor-bound holoenzyme was resolved at 2.0 Å; it contains two active site residues, Gly105 and Val322, specific for methionine γ-lyases. Modeling of methionine into the active site allows identification of the active site residues responsible for substrate recognition and catalysis. These findings support that CalE6 is a putative methionine γ-lyase producing methanethiol as a building block in biosynthesis of calicheamicins.

PubMed: 25404066
DOI: 10.1002/cbic.201402489

Experimental method

X-RAY DIFFRACTION (2 Å)