Brand  (β version)

PDB ID: 1ID8

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Ligands
Code Name Style Show Link
DBI Phosphoric acid mono-[5-(5,6-dimethyl-benzoimidazol-1-yl)-4-hydroxy-2-hydroxymethyl-tetrahydro-furan-3-yl] ester PoSSuM
FOP 2-hydroxy-propyl-ammonium PoSSuM
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Structure summary

Code : 1ID8   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : NMR STRUCTURE OF GLUTAMATE MUTASE (B12-BINDING SUBUNIT) COMPLEXED WITH THE VITAMIN B12 NUCLEOTIDE
Release Data : 2001-06-27
Compound :
mol_id molecule chains synonym
1 METHYLASPARTATE MUTASE S CHAIN A GLUTAMATE MUTASE
ec: 5.4.99.1
Source :
mol_id organism_scientific expression_system
1 Clostridium tetanomorphum  (taxid:1553) Escherichia coli BL21(DE3)  (taxid:469008)
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
expression_system_plasmid: PT7-7
Authors : Tollinger, M., Eichmuller, C., Konrat, R., Huhta, M.S., Marsh, E.N.G., Krautler, B.
Keywords : Coenzyme B12, Ligand Binding, Nucleotide, Protein NMR spectroscopy, Protein folding, ISOMERASE
Exp. method : SOLUTION NMR
Citation :

The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12).

Tollinger, M.,Eichmuller, C.,Konrat, R.  et al.
(2001)  J.Mol.Biol.  309 : 777 - 791

PubMed: 11397096
DOI: 10.1006/jmbi.2001.4696

Adenosylcobalamin-dependent Glutamate Mutase from Clostridium Tetanomorphum. Overexpression in Escherichia coli, Purification, and Characterization of the Recombinant Enzyme

Holloway, D.E.,Marsh, E.N.
(1994)  J.Biol.Chem.  269 : 20425 - 20430

How a Protein Prepares for B12 Binding: Structure and Dynamics of the B12-binding Subunit of Glutamate Mutase from Clostridium tetanomorphum

Tollinger, M.,Konrat, R.,Hilbert, B.H.  et al.
(1998)  Structure  6 : 1021 - 1033

DOI: 10.1016/S0969-2126(98)00103-8

Reaction

Chain : A
UniProt : Q05488 (GMSS_CLOTT)
Reaction: EC: Evidence:
Physiological Direction:
(2S,3S)-3-methyl-L-aspartate = L-glutamate 5.4.99.1 HAMAP-Rule:MF_00526, PubMed:8051138
-
Cofactor: Evidence: Note:
adenosylcob(III)alamin ECO:0000255 | HAMAP-Rule:MF_00526
ECO:0000269 | PubMed:8051138
-