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Structure paper

TitleA two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 24, Page 666-671, Year 2017
Publish dateJul 21, 2016 (structure data deposition date)
AuthorsRobertson, R.M. / Yao, J. / Gajewski, S. / Kumar, G. / Martin, E.W. / Rock, C.O. / White, S.W.
External linksNat. Struct. Mol. Biol. / PubMed:28714993
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-5kym:
Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-HGX:
1-HEPTADECANOYL-2-TRIDECANOYL-3-GLYCEROL-PHOSPHONYL CHOLINE

ChemComp-DD9:
nonane

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-HOH:
WATER

Source
  • thermotoga maritima (strain atcc 43589 / msb8 / dsm 3109 / jcm 10099) (bacteria)
KeywordsTRANSFERASE / integral membrane / membrane helices / HX4D acyltransferase / alpha-beta structure / 1-acyl-sn-glycerol-3-phosphate acyltransferase

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