2b4l

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Crystal structure of the binding protein OpuAC in complex with glycine betaineCrystal structure of the binding protein OpuAC in complex with glycine betaine

Structural highlights

2b4l is a 1 chain structure with sequence from Bacillus subtilis. 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

OPUAC_BACSU Involved in a multicomponent binding-protein-dependent transport system for glycine betaine.[1] [2]

Evolutionary Conservation

 

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

See Also

References

  1. Kempf B, Bremer E. OpuA, an osmotically regulated binding protein-dependent transport system for the osmoprotectant glycine betaine in Bacillus subtilis. J Biol Chem. 1995 Jul 14;270(28):16701-13. PMID:7622480
  2. Kappes RM, Kempf B, Bremer E. Three transport systems for the osmoprotectant glycine betaine operate in Bacillus subtilis: characterization of OpuD. J Bacteriol. 1996 Sep;178(17):5071-9. PMID:8752321

2b4l, resolution 2.00Å

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