1CCW

STRUCTURE OF THE COENZYME B12 DEPENDENT ENZYME GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM

Summary for 1CCW

Entry DOI	10.2210/pdb1ccw/pdb
Descriptor	PROTEIN (GLUTAMATE MUTASE), CYANOCOBALAMIN, D(-)-TARTARIC ACID, ... (5 entities in total)
Functional Keywords	glutamate mutase, coenzyme b12, radical reaction, tim-barrel, rossman-fold, isomerase
Biological source	Clostridium cochlearium More
Total number of polymer chains	4
Total formula weight	139919.36
Authors	Reitzer, R.,Gruber, K.,Kratky, C. (deposition date: 1999-03-01, release date: 2000-03-01, Last modification date: 2023-12-27)
Primary citation	Reitzer, R.,Gruber, K.,Jogl, G.,Wagner, U.G.,Bothe, H.,Buckel, W.,Kratky, C. Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights Structure Fold.Des., 7:891-902, 1999 Cited by PubMed Abstract: Glutamate mutase (Glm) equilibrates (S)-glutamate with (2S,3S)-3-methylaspartate. Catalysis proceeds with the homolytic cleavage of the organometallic bond of the cofactor to yield a 5'-desoxyadenosyl radical. This radical then abstracts a hydrogen atom from the protein-bound substrate to initiate the rearrangement reaction. Glm from Clostridium cochlearium is a heterotetrameric molecule consisting of two sigma and two epsilon polypeptide chains. PubMed: 10467146 DOI: 10.1016/S0969-2126(99)80116-6 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation