1cb7

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GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMINGLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN

Structural highlights

1cb7 is a 4 chain structure with sequence from Clostridium cochlearium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GMSS_CLOCO Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526][1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Leutbecher U, Bocher R, Linder D, Buckel W. Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors. Eur J Biochem. 1992 Apr 15;205(2):759-65. PMID:1315276
  2. ↑ Zelder O, Beatrix B, Leutbecher U, Buckel W. Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli. Eur J Biochem. 1994 Dec 1;226(2):577-85. PMID:7880251
  3. ↑ Zelder O, Beatrix B, Buckel W. Cloning, sequencing and expression in Escherichia coli of the gene encoding component S of the coenzyme B12-dependent glutamate mutase from Clostridium cochlearium. FEMS Microbiol Lett. 1994 May 1;118(1-2):15-21. PMID:8013871

1cb7, resolution 2.00Å

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OCA
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