title: Structural analysis of HopPmaL reveals the presence of a second adaptor domain common to the HopAB family of Pseudomonas syringae type III effectors.
abstract: HopPmaL is a member of the HopAB family of type III effectors present in the phytopathogen Pseudomonas syringae. Using both X-ray crystallography and solution nuclear magnetic resonance, we demonstrate that HopPmaL contains two structurally homologous yet functionally distinct domains. The N-terminal domain corresponds to the previously described Pto-binding domain, while the previously uncharacterised C-terminal domain spans residues 308-385. While structurally similar, these domains do not share significant sequence similarity and most importantly demonstrate significant differences in key residues involved in host protein recognition, suggesting that each of them targets a different host protein.
authors.affiliation: Department of Chemical Engineering and Applied Chemistry, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada.
authors.forename: Alex U
authors.initials: AU
authors.lastname: Singer
authors.forename: Bin
authors.initials: B
authors.lastname: Wu
authors.forename: Adelinda
authors.initials: A
authors.lastname: Yee
authors.forename: Scott
authors.initials: S
authors.lastname: Houliston
authors.forename: Xiaohui
authors.initials: X
authors.lastname: Xu
authors.forename: Hong
authors.initials: H
authors.lastname: Cui
authors.forename: Tatiana
authors.initials: T
authors.lastname: Skarina
authors.forename: Maite
authors.initials: M
authors.lastname: Garcia
authors.forename: Anthony
authors.initials: A
authors.lastname: Semesi
authors.forename: Cheryl H
authors.initials: CH
authors.lastname: Arrowsmith
authors.forename: Alexei
authors.initials: A
authors.lastname: Savchenko
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D057927:Hydrophobic and Hydrophilic Interactions; D018551:Solanum lycopersicum / Q000382:microbiology; D005810:Multigene Family; D010446:Peptide Fragments / Q000737:chemistry / Q000502:physiology; D010935:Plant Diseases / Q000382:microbiology; D010940:Plant Proteins / Q000737:chemistry; D011485:Protein Binding; D017510:Protein Folding; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry; D017434:Protein Structure, Tertiary; D044224:Pseudomonas syringae / Q000737:chemistry* / Q000472:pathogenicity*; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D010446:Peptide Fragments; D010940:Plant Proteins; C081695:avrPto protein, Pseudomonas syringae; C084354:Pto protein, Lycopersicon; D017346:Protein Serine-Threonine Kinases