|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.
|chemistry physiology pathogenicity microbiology |
|Crystallography, X-Ray Protein Structure, Tertiary Conserved Sequence Protein Binding Sequence Alignment Protein Folding Bacterial Proteins Hydrophobic and Hydrophilic Interactions Multigene Family Plant Proteins Peptide Fragments Protein-Serine-Threonine Kinases Pseudomonas syringae Plant Diseases Lycopersicon esculentum |
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