Literature summary for 2.7.4.3 extracted from

Arora, K.; Brooks, C.L.
Large-scale allosteric conformational transitions of adenylate kinase appear to involve a population-shift mechanism (2007), Proc. Natl. Acad. Sci. USA, 104, 18496-18501.

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of atomically detailed conformational transition pathway of adenylate kinase in the absence and presence of an inhibitor. In the ligand-free state, there is no significant barrier separating the open and closed conformations. The enzyme samples near closed conformations, even in the absence of its substrate. The ligand binding event occurs late, toward the closed state, and transforms the free energy landscape. In the ligand-bound state, the closed conformation is energetically most favored with a large barrier to opening	Escherichia coli

Crystallization (Comment)

Organism

analysis of atomically detailed conformational transition pathway of adenylate kinase in the absence and presence of an inhibitor. In the ligand-free state, there is no significant barrier separating the open and closed conformations. The enzyme samples near closed conformations, even in the absence of its substrate. The ligand binding event occurs late, toward the closed state, and transforms the free energy landscape. In the ligand-bound state, the closed conformation is energetically most favored with a large barrier to opening

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P69441	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)