Literature summary for 4.2.2.2 extracted from

Dehdashti, S.J.; Doan, C.N.; Chao, K.L.; Yoder, M.D.
Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16 (2003), Acta Crystallogr. Sect. D, 59, 1339-1342.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapor-diffusion method, crystal structure of the PelA T1.5 mutant solved to 1.6 and 2.9 A resolution. Four residues in the T1.5 loop region of PelA are mutated (N215S, T217S, S219G and A220S) to match the structurally analogous T1.5 loop of PelE	Dickeya chrysanthemi

Protein Variants

Protein Variants	Comment	Organism
N215S/T217S/S219G/A220S	the four residues in the T1.5 loop region of PelA are mutated to match the structurally analogous T1.5 loop of PelE. Mutant enzyme shows a conformational change in the T1.5 loop from PelA conformation to that observed in pelE. The pH-optimum of the mutant enzyme is identical to that of PelA, but the T1.5 mutant has an increased specific activity that is comparable to that of PelE	Dickeya chrysanthemi

Organism

Organism	UniProt	Comment	Textmining
Dickeya chrysanthemi	-	EC16	-
Dickeya chrysanthemi EC16	-	EC16	-

Synonyms

Synonyms	Comment	Organism
PelA	-	Dickeya chrysanthemi

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Release 2023.1 (January 2023)