1r5e

Solution structure of the folded core of Pseudomonas syringae effector protein, AvrPtoSolution structure of the folded core of Pseudomonas syringae effector protein, AvrPto

Structural highlights 1r5e is a 1 chain structure with sequence from Pseudomonas syringae. 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 Q08242_PSESX Publication Abstract from PubMed Pseudomonas syringae pv. tomato, the causative agent of bacterial speck disease of tomato, uses a type III secretion system (TTSS) to deliver effector proteins into the host cell. In resistant plants, the bacterial effector protein AvrPto physically interacts with the host Pto kinase and elicits antibacterial defense responses. In susceptible plants, which lack the Pto kinase, AvrPto acts as a virulence factor to promote bacterial growth. The solution structure of AvrPto reveals a functional core consisting of a three-helix bundle motif flanked by disordered N- and C-terminal tails. Residues required for Pto binding lie in a 19 residue Omega loop. Modeling suggests a hydrophobic patch involving the activation loop of Pto forms a contact surface with the AvrPto Omega loop and that helix packing mediates interactions between AvrPto and putative virulence targets Api2 and Api3. The AvrPto structure has a low stability that may facilitate chaperone-independent secretion by the TTSS. The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis.,Wulf J, Pascuzzi PE, Fahmy A, Martin GB, Nicholson LK Structure. 2004 Jul;12(7):1257-68. PMID:15242602 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avirulence protein 3D structures

spinqualitylabelsall models 1r5e Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image