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Structure paper

TitleStructure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page 2218-2223, Year 2017
Publish dateDec 21, 2015 (structure data deposition date)
AuthorsAnandan, A. / Evans, G.L. / Condic-Jurkic, K. / O'Mara, M.L. / John, C.M. / Phillips, N.J. / Jarvis, G.A. / Wills, S.S. / Stubbs, K.A. / Moraes, I. ...Anandan, A. / Evans, G.L. / Condic-Jurkic, K. / O'Mara, M.L. / John, C.M. / Phillips, N.J. / Jarvis, G.A. / Wills, S.S. / Stubbs, K.A. / Moraes, I. / Kahler, C.M. / Vrielink, A.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:28193899
MethodsX-ray diffraction
Resolution2.75 Å
Structure data

PDB-5fgn:
Integral membrane protein lipooligosaccharide phosphoethanolamine transferase A (EptA) from Neisseria meningitidis
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-BGL:
2-O-octyl-beta-D-glucopyranose / detergent*YM

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

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • neisseria meningitidis serogroup b (bacteria)
KeywordsTRANSFERASE / HYDROLASE / Endotoxin Biosynthesis / EptA / Membrane protein / Phosphoethanolamine transferase / Polymixin Resistance / Phosphotransferase

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