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Literature summary for 5.4.99.1 extracted from

  • 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 (1998), Structure, 15, 1021-1033.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Clostridium tetanomorphum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14800
-
2 * 14800, B12-binding component S, + 2 * 53700, component E Clostridium tetanomorphum
53700
-
2 * 14800, B12-binding component S, + 2 * 53700, component E Clostridium tetanomorphum

Organism

Organism UniProt Comment Textmining
Clostridium tetanomorphum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Glu
-
Clostridium tetanomorphum threo-3-Methylaspartate
-
?

Subunits

Subunits Comment Organism
tetramer 2 * 14800, B12-binding component S, + 2 * 53700, component E Clostridium tetanomorphum

Cofactor

Cofactor Comment Organism Structure
Cobalamin dependent on Clostridium tetanomorphum
Cobalamin the major part of component S is preorganized for vitamin B12 binding, but the B12-binding site itself is only partially formed. Upon binding B12, important elements of the binding site appear to become structured, including an alpha-helix that forms one side of the cleft accomodating the nucleotide 'tail' of the cofactor Clostridium tetanomorphum