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TitleStructure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateAug 17, 2020 (structure data deposition date)
AuthorsBryant, J.A. / Morris, F.C. / Knowles, T.J. / Maderbocus, R. / Heinz, E. / Boelter, G. / Alodaini, D. / Colyer, A. / Wotherspoon, P.J. / Staunton, K.A. ...Bryant, J.A. / Morris, F.C. / Knowles, T.J. / Maderbocus, R. / Heinz, E. / Boelter, G. / Alodaini, D. / Colyer, A. / Wotherspoon, P.J. / Staunton, K.A. / Jeeves, M. / Browning, D.F. / Sevastsyanovich, Y.R. / Wells, T.J. / Rossiter, A.E. / Bavro, V.N. / Sridhar, P. / Ward, D.G. / Chong, Z.S. / Goodall, E.C. / Icke, C. / Teo, A.C. / Chng, S.S. / Roper, D.I. / Lithgow, T. / Cunningham, A.F. / Banzhaf, M. / Overduin, M. / Henderson, I.R.
External linksElife / PubMed:33315009
MethodsNMR (solution)
Structure data

PDB-7a2d:
Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation to the cell division site
Method: SOLUTION NMR

Source
  • escherichia coli (strain k12) (bacteria)
KeywordsPROTEIN BINDING / OUTER MEMBRANE BIOGENESIS / GRAM NEGATIVE / LIPOPROTEIN / YRAP / LIPID BIOGENESIS

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