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TitleA broader active site inPyrococcus horikoshiiCoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry.
Journal, issue, pagesFEBS Open Bio, Vol. 8, Page 1083-1092, Year 2018
Publish dateJul 29, 2016 (structure data deposition date)
AuthorsSea, K. / Lee, J. / To, D. / Chen, B. / Sazinsky, M.H. / Crane, E.J.
External linksFEBS Open Bio / PubMed:29988575
MethodsX-ray diffraction
Resolution3.6 Å
Structure data

PDB-5l1n:
Pyrococcus horikoshii CoA Disulfide Reductase Quadruple Mutant
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-COA:
COENZYME A

Source
  • pyrococcus horikoshii (archaea)
KeywordsOXIDOREDUCTASE / sulfur metabolism half-sites reactivity

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