1BE1

GLUTAMATE MUTASE (B12-BINDING SUBUNIT), NMR, MINIMIZED AVERAGE STRUCTURE

Summary for 1BE1

• Entry DOI: 10.2210/pdb1be1/pdb
• Descriptor: GLUTAMATE MUTASE (1 entity in total)
• Functional Keywords: isomerase, glutamate mutase, b12-binding subunit
• Biological source: Clostridium tetanomorphum
• Total number of polymer chains: 1
• Total formula weight: 14763.86

Authors

Tollinger, M.,Konrat, R.,Hilbert, B.H.,Marsh, E.N.G.,Kraeutler, B. (deposition date: 1998-05-19, release date: 1998-08-26, Last modification date: 2024-05-22)

Primary citation

Tollinger, M.,Konrat, R.,Hilbert, B.H.,Marsh, E.N.,Krautler, B.
How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum
Structure, 6:1021-1033, 1998

PubMed Abstract: Glutamate mutase is an adenosylcobamide (coenzyme B12) dependent enzyme that catalyzes the reversible rearrangement of (2S)-glutamate to (2S,3S)-3-methylaspartate. The enzyme from Clostridium tetanomorphum comprises two subunits (of 53.7 and 14.8 kDa) and in its active form appears to be an alpha 2 beta 2 tetramer. The smaller subunit, termed MutS, has been characterized as the B12-binding component. Knowledge on the structure of a B12-binding apoenzyme does not exist.

PubMed: 9739092
DOI: 10.1016/S0969-2126(98)00103-8

Experimental method

SOLUTION NMR