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Structure paper

TitleThe role of OleA His285 in orchestration of long-chain acyl-coenzyme A substrates.
Journal, issue, pagesFEBS Lett., Vol. 592, Page 987-998, Year 2018
Publish dateSep 20, 2017 (structure data deposition date)
AuthorsJensen, M.R. / Goblirsch, B.R. / Esler, M.A. / Christenson, J.K. / Mohamed, F.A. / Wackett, L.P. / Wilmot, C.M.
External linksFEBS Lett. / PubMed:29430657
MethodsX-ray diffraction
Resolution1.77 - 2.8 Å
Structure data

PDB-6b2r:
Crystal structure of Xanthomonas campestris OleA H285A
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

PDB-6b2s:
Crystal structure of Xanthomonas campestris OleA H285N
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6b2t:
Crystal structure of Xanthomonas campestris OleA H285D
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • xanthomonas campestris pv. campestris (strain atcc 33913 / dsm 3586 / ncppb 528 / lmg 568 / p 25) (bacteria)
KeywordsTRANSFERASE / Thiolase / OleA / Condensation

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