3SVI

Structure of the Pto-binding domain of HopPmaL generated by limited thermolysin digestion

Summary for 3SVI

• Entry DOI: 10.2210/pdb3svi/pdb
• Descriptor: Type III effector HopAB2, SULFATE ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: type iii effector, structural genomics, psi-biology, midwest center for structural genomics, mcsg, helical bundle, signaling protein
• Biological source: Pseudomonas syringae
• Total number of polymer chains: 1
• Total formula weight: 9938.28

Authors

Singer, A.U.,Stein, A.,Xu, X.,Cui, H.,Joachimiak, A.,Edwards, A.M.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2011-07-12, release date: 2011-08-10, Last modification date: 2024-11-20)

Primary citation

Singer, A.U.,Wu, B.,Yee, A.,Houliston, S.,Xu, X.,Cui, H.,Skarina, T.,Garcia, M.,Semesi, A.,Arrowsmith, C.H.,Savchenko, A.
Structural Analysis of HopPmaL Reveals the Presence of a Second Adaptor Domain Common to the HopAB Family of Pseudomonas syringae Type III Effectors.
Biochemistry, 51:1-3, 2012

PubMed 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.

PubMed: 22191472
DOI: 10.1021/bi2013883

Experimental method

X-RAY DIFFRACTION (1.8 Å)