|Biochemistry (2012) 51:1-3|
|Northeast Structural Genomics Consortium|
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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.
|microbiology chemistry physiology pathogenicity |
|Crystallography, X-Ray Protein Structure, Tertiary Conserved Sequence Multigene Family Plant Diseases Sequence Alignment Lycopersicon esculentum Protein-Serine-Threonine Kinases Plant Proteins Protein Folding Protein Binding Bacterial Proteins Pseudomonas syringae Hydrophobic and Hydrophilic Interactions Peptide Fragments |
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