Literature summary for 4.2.2.2 extracted from

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 (2008), J. Biol. Chem., 283, 18260-18268.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Dickeya chrysanthemi

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of PelI is 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. The structure of PelI in complex with its substrate, a tetragalacturonate, is 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 are consistent with the dual mode of bond cleavage in this substrate. The bound sugar adopts a mixed 21 and 31 helical conformation similar to that reported in inactive mutants from families PL-1 and PL-10	Dickeya chrysanthemi

Crystallization (Comment)

Organism

crystal structure of PelI is 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. The structure of PelI in complex with its substrate, a tetragalacturonate, is 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 are consistent with the dual mode of bond cleavage in this substrate. The bound sugar adopts a mixed 21 and 31 helical conformation similar to that reported in inactive mutants from families PL-1 and PL-10

Dickeya chrysanthemi

Protein Variants

Protein Variants	Comment	Organism
K224R	mutant is completely defective in lyase activity	Dickeya chrysanthemi
K249R	mutant shows 40-60% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected	Dickeya chrysanthemi
R252K	mutant shows 6-9% of wild-type activity. At a higher Ca2+ concentration in the substrate medium, enzymatic activities of K249R and R252K mutants are less affected	Dickeya chrysanthemi

Organism

Organism	UniProt	Comment	Textmining
Dickeya chrysanthemi	O50325	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pectin	-	Dickeya chrysanthemi	?	-	?

Synonyms

Synonyms	Comment	Organism
pectate lyase	-	Dickeya chrysanthemi
PelI	-	Dickeya chrysanthemi
PL-3	-	Dickeya chrysanthemi

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Dickeya chrysanthemi

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	assay at	Dickeya chrysanthemi