1ooc | pdb_00001ooc

Mutations in the T1.5 loop of pectate lyase A

spinqualitylabelsall models 1ooc, resolution 2.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ooc is a 2 chain structure with sequence from Dickeya chrysanthemi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.94Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLYA_DICCH Involved in maceration and soft-rotting of plant tissue. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Pectate lyase A (PelA) is a pectate-degrading enzyme secreted by plant pathogens. PelA from Erwinia chrysanthemi has 61% amino-acid identity and a conserved structural similarity to pectate lyase E (PelE). Although similar in structure and sequence, the enzymatic characteristics of PelA differ from those for PelE. A structural alignment of PelA and PelE reveals differences in the T1.5 loop. The sequence of the T1.5 loop in PelA was mutated to the homologous sequence in PelE. The crystal structure of the PelA T1.5 mutant has been solved to 1.6 and 2.9 A resolution. The enzymatic and structural properties of the T1.5 mutant are discussed. Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16.,Dehdashti SJ, Doan CN, Chao KL, Yoder MD Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1339-42. Epub 2003, Jun 27. PMID:12832805 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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