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TitleThe Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells.
Journal, issue, pagesPlos Pathog., Vol. 12, Page e1005919-e1005919, Year 2016
Publish dateApr 25, 2016 (structure data deposition date)
AuthorsParker, M.L. / Houston, S. / Petrosova, H. / Lithgow, K.V. / Hof, R. / Wetherell, C. / Kao, W.C. / Lin, Y.P. / Moriarty, T.J. / Ebady, R. ...Parker, M.L. / Houston, S. / Petrosova, H. / Lithgow, K.V. / Hof, R. / Wetherell, C. / Kao, W.C. / Lin, Y.P. / Moriarty, T.J. / Ebady, R. / Cameron, C.E. / Boulanger, M.J.
External linksPlos Pathog. / PubMed:27683203
MethodsX-ray diffraction
Resolution2.15 Å
Structure data

PDB-5jk2:
Crystal structure of Treponema pallidum Tp0751 (Pallilysin)
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • treponema pallidum (strain nichols) (bacteria)
KeywordsCELL ADHESION / Lipocalin / outer membrane protein / adhesin

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