Literature summary for 2.7.4.3 extracted from

Whitford, P.C.; Miyashita, O.; Levy, Y.; Onuchic, J.N.
Conformational transitions of adenylate kinase: switching by cracking (2007), J. Mol. Biol., 366, 1661-1671.

Crystallization (Commentary)

Crystallization (Comment)	Organism
coarse-grained models and nonlinear normal mode analysis. Intrinsic structural fluctuations dominate LID domain motion, whereas ligand-protein interactions and local unfolding are more important during NMP domain motion. LID-NMP domain interactions are indispensable for efficient catalysis. LID domain motion precedes NMP domain motion, during both opening and closing, providing mechanistic explanation for the observed 1:1:1 correspondence between LID domain closure, NMP domain closure, and substrate turnover	Escherichia coli

Crystallization (Comment)

Organism

coarse-grained models and nonlinear normal mode analysis. Intrinsic structural fluctuations dominate LID domain motion, whereas ligand-protein interactions and local unfolding are more important during NMP domain motion. LID-NMP domain interactions are indispensable for efficient catalysis. LID domain motion precedes NMP domain motion, during both opening and closing, providing mechanistic explanation for the observed 1:1:1 correspondence between LID domain closure, NMP domain closure, and substrate turnover

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P69441	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + AMP = 2 ADP	coarse-grained models and nonlinear normal mode analysis. Intrinsic structural fluctuations dominate LID domain motion, whereas ligand-protein interactions and local unfolding are more important during NMP domain motion. LID-NMP domain interactions are indispensable for efficient catalysis. LID domain motion precedes NMP domain motion, during both opening and closing, providing mechanistic explanation for the observed 1:1:1 correspondence between LID domain closure, NMP domain closure, and substrate turnover	Escherichia coli	a

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)