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Structure paper

TitleConformational changes in Apolipoprotein N-acyltransferase (Lnt).
Journal, issue, pagesSci Rep, Vol. 10, Page 639-639, Year 2020
Publish dateFeb 7, 2019 (structure data deposition date)
AuthorsWiseman, B. / Hogbom, M.
External linksSci Rep / PubMed:31959792
MethodsX-ray diffraction
Resolution3.1 - 3.5 Å
Structure data

PDB-6nwr:
Thioester acyl-intermediate of Apolipoprotein N-acyltransferase (Lnt)
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

PDB-6q3a:
Apo form of Apolipoprotein N-acyltransferase (Lnt)
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

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

ChemComp-D12:
DODECANE

ChemComp-GOL:
GLYCEROL

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

Source
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli k-12 (bacteria)
KeywordsMEMBRANE PROTEIN / Enzyme / Nitrilase / N-acyltransferase / Lipoprotein / lipoproteins / biosynthetic protein

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