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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.

SUBMITTER: Singer AU 

PROVIDER: S-EPMC3656468 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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Structural analysis of HopPmaL reveals the presence of a second adaptor domain common to the HopAB family of Pseudomonas syringae type III effectors.

Singer Alex U AU   Wu Bin B   Yee Adelinda A   Houliston Scott S   Xu Xiaohui X   Cui Hong H   Skarina Tatiana T   Garcia Maite M   Semesi Anthony A   Arrowsmith Cheryl H CH   Savchenko Alexei A  

Biochemistry 20111228 1


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 sha  ...[more]

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