1CB7

GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN

Summary for 1CB7

Entry DOI	10.2210/pdb1cb7/pdb
Descriptor	PROTEIN (GLUTAMATE MUTASE), CO-METHYLCOBALAMIN, 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	139895.37
Authors	Gruber, K.,Reitzer, R.,Kratky, C. (deposition date: 1999-03-03, release date: 2000-02-28, Last modification date: 2024-04-03)
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 (2 Å)

Structure validation