3b4n

Crystal Structure Analysis of Pectate Lyase PelI from Erwinia chrysanthemi

spinqualitylabelsall models 3b4n, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b4n is a 2 chain structure with sequence from "erwinia_carotovora_var._chrysanthemi"_(burkholder_et_al._1953)_dye_1969 "erwinia carotovora var. chrysanthemi" (burkholder et al. 1953) dye 1969. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, EDO, SO4, ZN Related: 3b8y Gene: pelI ("Erwinia carotovora var. chrysanthemi" (Burkholder et al. 1953) Dye 1969) Activity: Pectate lyase, with EC number 4.2.2.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 The crystallographic structure of the family 3 polysaccharide lyase (PL-3) PelI from Erwinia chrysanthemi has been solved to 1.45 A resolution. It consists of an N-terminal domain harboring a fibronectin type III fold linked to a catalytic domain displaying a parallel beta-helix topology. The N-terminal domain is located away from the active site and is not involved in the catalytic process. After secretion in planta, the two domains are separated by E. chrysanthemi proteases. This event turns on the hypersensitive response of the host. The structure of the single catalytic domain determined to 2.1 A resolution shows that the domain separation unveils a "Velcro"-like motif of asparagines, which might be recognized by a plant receptor. The structure of PelI in complex with its substrate, a tetragalacturonate, has been solved to 2.3 A resolution. The sugar binds from subsites -2 to +2 in one monomer of the asymmetric unit, although it lies on subsites -1 to +3 in the other. These two "Michaelis complexes" have never been observed simultaneously before and are consistent with the dual mode of bond cleavage in this substrate. The bound sugar adopts a mixed 2(1) and 3(1) helical conformation similar to that reported in inactive mutants from families PL-1 and PL-10. However, our study suggests that the catalytic base in PelI is not a conventional arginine but a lysine as proposed in family PL-9. The crystal structure of pectate lyase peli from soft rot pathogen Erwinia chrysanthemi in complex with its substrate.,Creze C, Castang S, Derivery E, Haser R, Hugouvieux-Cotte-Pattat N, Shevchik VE, Gouet P J Biol Chem. 2008 Jun 27;283(26):18260-8. Epub 2008 Apr 22. PMID:18430740 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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