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Structure paper

TitleSubstrate Trapping in Crystals of the Thiolase OleA Identifies Three Channels That Enable Long Chain Olefin Biosynthesis.
Journal, issue, pagesJ. Biol. Chem., Vol. 291, Page 26698-26706, Year 2016
Publish dateMay 20, 2013 (structure data deposition date)
AuthorsGoblirsch, B.R. / Jensen, M.R. / Mohamed, F.A. / Wackett, L.P. / Wilmot, C.M.
External linksJ. Biol. Chem. / PubMed:27815501
MethodsX-ray diffraction
Resolution1.839 - 2.36 Å
Structure data

PDB-4kti:
Crystal Structure of C143A Xathomonas campestris OleA
Method: X-RAY DIFFRACTION / Resolution: 1.839 Å

PDB-4ktm:
Crystal Structure of C143S Xanthomonas campestris OleA
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

PDB-4ku2:
Crystal Structure C143A from Xanthomonas campestris Bound with Myristoyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 1.974 Å

PDB-4ku3:
Crystal Structure of C143S Xanthomonas Campestris OleA bound with myristic acid and myrisotoyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 1.97 Å

PDB-4ku5:
Crystal Structures of C143S Xanthomonas campestris OleA with Bound Lauric Acid and Lauroyl-CoA
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MYA:
TETRADECANOYL-COA

ChemComp-MYR:
MYRISTIC ACID

ChemComp-DAO:
LAURIC ACID

ChemComp-DCC:
DODECYL-COA

Source
  • xanthomonas campestris pv. campestris (bacteria)
KeywordsTRANSFERASE / Thiolase

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