2lf3

Solution NMR structure of HopPmaL_281_385 from Pseudomonas syringae pv. maculicola str. ES4326, Midwest Center for Structural Genomics target APC40104.5 and Northeast Structural Genomics Consortium target PsT2ASolution NMR structure of HopPmaL_281_385 from Pseudomonas syringae pv. maculicola str. ES4326, Midwest Center for Structural Genomics target APC40104.5 and Northeast Structural Genomics Consortium target PsT2A

Structural highlights 2lf3 is a 1 chain structure with sequence from Pseudomonas syringae pv. maculicola. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HPAB3_PSEYM Effector protein involved in gene-for-gene resistance in tomato plants. It is recognized by the host Pto resistance protein and elicits Pto and Prf-dependent hypersensitive response (HR) and programmed cell death (PCD), resulting in host immunity. In susceptible plants, promotes virulence, in part, by enhancing the development of disease symptoms and bacterial growth. Publication Abstract from PubMed 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. Structural Analysis of HopPmaL Reveals the Presence of a Second Adaptor Domain Common to the HopAB Family of Pseudomonas syringae Type III Effectors.,Singer AU, Wu B, Yee A, Houliston S, Xu X, Cui H, Skarina T, Garcia M, Semesi A, Arrowsmith CH, Savchenko A Biochemistry. 2012 Jan 10;51(1):1-3. Epub 2011 Dec 28. PMID:22191472 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avirulence protein 3D structures

spinqualitylabelsall models 2lf3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image