Proteopedia

2b4l

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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