Literature summary for 6.3.2.4 extracted from

Kitamura, Y.; Ebihara, A.; Agari, Y.; Shinkai, A.; Hirotsu, K.; Kuramitsu, S.
Structure of D-alanine-D-alanine ligase from Thermus thermophilus HB8: cumulative conformational change and enzyme-ligand interactions (2009), Acta Crystallogr. Sect. D, 65, 1098-1106.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of unliganded enzyme to 2.3 A resolution, of Ddl with adenylyl imidodiphosphate to 2.6 A resolution, of Ddl with ADP to 2.2 A resolution, of Ddl with ADP and D-Ala to 1.9 A resolution, and of Ddl with ATP and D-Ala-D-Ala to 2.3 A resolution. The central domain rotates as a rigid body towards the active site in a cumulative manner in concert with the local conformational change of three flexible loops depending upon substrate or product binding, resulting in an overall structural change from the open to the closed form through semi-open and semi-closed forms	Thermus thermophilus HB8

Crystallization (Comment)

Organism

structure of unliganded enzyme to 2.3 A resolution, of Ddl with adenylyl imidodiphosphate to 2.6 A resolution, of Ddl with ADP to 2.2 A resolution, of Ddl with ADP and D-Ala to 1.9 A resolution, and of Ddl with ATP and D-Ala-D-Ala to 2.3 A resolution. The central domain rotates as a rigid body towards the active site in a cumulative manner in concert with the local conformational change of three flexible loops depending upon substrate or product binding, resulting in an overall structural change from the open to the closed form through semi-open and semi-closed forms

Thermus thermophilus HB8

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus HB8	Q5SHZ3	-	-

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Release 2023.1 (January 2023)