Literature summary for 4.2.99.20 extracted from

Johnston, J.M.; Jiang, M.; Guo, Z.; Baker, E.N.
Crystal structures of E. coli native MenH and two active site mutants (2013), PLoS ONE, 8, e61325.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
native enzyme to 2.75 A resolution, together with the structures of the active site mutant proteins Tyr85Phe and Arg124Ala, both at 2.5 A resolution. The enzyme has the predicted alpha/beta hydrolase fold with its core alpha/beta domain capped by a helical lid. The active site, a long groove beneath the cap, contains a number of conserved basic residues and is found to bind exogeneous anions, modeled as sulfate and chloride, in all three crystal structures. The bound anions may mark the binding sites for anionic groups on the substrate	Escherichia coli

Crystallization (Comment)

Organism

native enzyme to 2.75 A resolution, together with the structures of the active site mutant proteins Tyr85Phe and Arg124Ala, both at 2.5 A resolution. The enzyme has the predicted alpha/beta hydrolase fold with its core alpha/beta domain capped by a helical lid. The active site, a long groove beneath the cap, contains a number of conserved basic residues and is found to bind exogeneous anions, modeled as sulfate and chloride, in all three crystal structures. The bound anions may mark the binding sites for anionic groups on the substrate

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P37355	-	-

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Release 2023.1 (January 2023)