3B90
Crystal Structure of the Catalytic Domain of Pectate Lyase PelI from Erwinia chrysanthemi
Summary for 3B90
| Entry DOI | 10.2210/pdb3b90/pdb |
| Related | 3B4N 3B8Y |
| Descriptor | Endo-pectate lyase, CALCIUM ION, ZINC ION, ... (5 entities in total) |
| Functional Keywords | pectate lyase, pectin, galacturonic acid, erwinia chrysanthemi, right-handed parallel beta helix fold, catalytic domain, lyase |
| Biological source | Erwinia chrysanthemi |
| Total number of polymer chains | 2 |
| Total formula weight | 48237.29 |
| Authors | Creze, C.,Castang, S.,Derivery, E.,Haser, R.,Shevchik, V.,Gouet, P. (deposition date: 2007-11-02, release date: 2008-04-29, Last modification date: 2011-07-13) |
| Primary citation | Creze, C.,Castang, S.,Derivery, E.,Haser, R.,Hugouvieux-Cotte-Pattat, N.,Shevchik, V.E.,Gouet, P. The Crystal Structure of Pectate Lyase PelI from Soft Rot Pathogen Erwinia chrysanthemi in Complex with Its Substrate J.Biol.Chem., 283:18260-18268, 2008 Cited by PubMed Abstract: 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. PubMed: 18430740DOI: 10.1074/jbc.M709931200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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