X-ray Crystallographic Structure of BshC, a Unique Enzyme Involved in Bacillithiol Biosynthesis

@inproceedings{VanDuinen2015XrayCS,
  title={X-ray Crystallographic Structure of BshC, a
Unique Enzyme Involved in Bacillithiol Biosynthesis},
  author={Andrew J. VanDuinen and Kelsey R. Winchell and Mary E. Keithly and P. Dan Cook},
  booktitle={Biochemistry},
  year={2015}
}
Bacillithiol is produced by many Gram-positive bacteria via a pathway utilizing the enzymes BshA, BshB, and BshC. Here we report the 1.77 Å resolution crystal structure of BshC, the putative cysteine ligase in bacillithiol production. The structure reveals that BshC contains a core Rossmann fold with connecting peptide motifs (CP1 and CP2) and a unique α-helical coiled-coil domain that facilitates dimerization. The model contains citrate and glycerol in the canonical active site and ADP in a… CONTINUE READING

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References

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Showing 1-10 of 22 references

Structure and function of the genomically

  • R N.
  • 2014
1 Excerpt

Features and development of Coot

  • A. Vagin, A. Teplyakov
  • Acta Crystallogr D Biol Crystallogr
  • 2010

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