spacer
spacer

PDBsum entry 1fmf

Go to PDB code: 
protein links
Isomerase PDB id
1fmf
Jmol
Contents
Protein chain
137 a.a. *
* Residue conservation analysis
PDB id:
1fmf
Name: Isomerase
Title: Refined solution structure of the (13c,15n-labeled) b12- binding subunit of glutamate mutase from clostridium tetanomorphum
Structure: Methylaspartate mutase s chain. Chain: a. Synonym: glutamate mutase, muts. Engineered: yes
Source: Clostridium tetanomorphum. Organism_taxid: 1553. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 30 models
Authors: B.Hoffmann,R.Konrat,M.Tollinger,M Huhta,E.N.G.Marsh, B.Kraeutler
Key ref: B.Hoffmann et al. (2001). A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum. Chembiochem, 2, 643-655. PubMed id: 11828501 DOI: 10.1002/1439-7633(20010903)2:9<643::AID-CBIC643>3.0.CO;2-J
Date:
17-Aug-00     Release date:   15-Feb-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q05488  (MAMA_CLOTT) -  Glutamate mutase sigma subunit
Seq:
Struc:
137 a.a.
137 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.4.99.1  - Methylaspartate mutase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-threo-3-methylaspartate = L-glutamate
L-threo-3-methylaspartate
= L-glutamate
      Cofactor: Cob(II)alamin
Cob(II)alamin
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     anaerobic glutamate catabolic process   2 terms 
  Biochemical function     isomerase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1002/1439-7633(20010903)2:9<643::AID-CBIC643>3.0.CO;2-J Chembiochem 2:643-655 (2001)
PubMed id: 11828501  
 
 
A protein pre-organized to trap the nucleotide moiety of coenzyme B(12): refined solution structure of the B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum.
B.Hoffmann, M.Tollinger, R.Konrat, M.Huhta, E.N.Marsh, B.Kräutler.
 
  ABSTRACT  
 
Uniformly (13)C,(15)N-labeled MutS, the coenzyme B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum, was prepared by overexpression from an Escherichia coli strain. Multidimensional heteronuclear NMR spectroscopic experiments with aqueous solutions of (13)C,(15)N-labeled MutS provided signal assignments for roughly 90% of the 1025 hydrogen, 651 carbon, and 173 nitrogen atoms and resulted in about 1800 experimental restraints. Based on the information from the NMR experiments, the structure of MutS was calculated, confirming the earlier, less detailed structure obtained with (15)N-labeled MutS. The refined analysis allowed a precise determination of the secondary and tertiary structure including several crucial side chain interactions. The structures of (the apoprotein) MutS in solution and of the B(12)-binding subunit in the crystal of the corresponding homologous holoenzyme from Clostridium cochlearium differ only in a section that forms the well-structured helix alpha1 in the crystal structure and that also comprises the cobalt-coordinating histidine residue. In the apoprotein MutS, this part of the B(12)-binding subunit is dynamic. The carboxy-terminal end of this section is conformationally flexible and has significant propensity for an alpha-helical structure ("nascent helix"). This dynamic section in MutS is a decisive element for the binding of the nucleotide moiety of coenzyme B(12) and appears to be stabilized as a helix (alpha1) upon trapping of the nucleotide of the B(12) cofactor.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
12413543 K.Gruber, and C.Kratky (2002).
Coenzyme B(12) dependent glutamate mutase.
  Curr Opin Chem Biol, 6, 598-603.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.