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Structure paper

TitleStructural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page E6044-E6053, Year 2017
Publish dateMay 10, 2017 (structure data deposition date)
AuthorsNoland, C.L. / Kattke, M.D. / Diao, J. / Gloor, S.L. / Pantua, H. / Reichelt, M. / Katakam, A.K. / Yan, D. / Kang, J. / Zilberleyb, I. ...Noland, C.L. / Kattke, M.D. / Diao, J. / Gloor, S.L. / Pantua, H. / Reichelt, M. / Katakam, A.K. / Yan, D. / Kang, J. / Zilberleyb, I. / Xu, M. / Kapadia, S.B. / Murray, J.M.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:28698362
MethodsX-ray diffraction
Resolution2.137 - 2.518 Å
Structure data

PDB-5vrg:
Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase
Method: X-RAY DIFFRACTION / Resolution: 2.518 Å

PDB-5vrh:
Apolipoprotein N-acyltransferase C387S active site mutant
Method: X-RAY DIFFRACTION / Resolution: 2.137 Å

Chemicals

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

ChemComp-LNK:
PENTANE

ChemComp-PLM:
PALMITIC ACID

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-OLB:
(2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (strain k12) (bacteria)
KeywordsTRANSFERASE / Lnt / acyl transferase / membrane protein / Lnt C387S

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