Literature summary for 4.2.1.20 extracted from

Nishio, K.; Ogasahara, K.; Morimoto, Y.; Tsukihara, T.; Lee, S.J.; Yutani, K.
Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5-phosphate binding (2010), FEBS J., 277, 2157-2170.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of apo-beta2 and holo-beta2 from Escherichia coli is determined at 3.0 and 2.9 A resolutions. The apo-type and holo-type molecule retain a dimeric form in solution. The subunit structures of both the apo-beta2 and the holo-beta2 forms consist of two domains, (N domain, C domain). The pyridoxal 5-phosphate-bound holo-form has multiple interactions between the two domains and a long loop (residues 260-310), which are missing in the apo-form	Escherichia coli

Crystallization (Comment)

Organism

crystal structures of apo-beta2 and holo-beta2 from Escherichia coli is determined at 3.0 and 2.9 A resolutions. The apo-type and holo-type molecule retain a dimeric form in solution. The subunit structures of both the apo-beta2 and the holo-beta2 forms consist of two domains, (N domain, C domain). The pyridoxal 5-phosphate-bound holo-form has multiple interactions between the two domains and a long loop (residues 260-310), which are missing in the apo-form

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A879	-	-

Subunits

Subunits	Comment	Organism
homodimer	crystal structure	Escherichia coli

Synonyms

Synonyms	Comment	Organism
tryptophan synthase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	crystal structures of apo-beta2 and holo-beta2 from Escherichia coli is determined at 3.0 and 2.9 A resolutions. The apo-type and holo-type molecule retain a dimeric form in solution. The subunit structures of both the apo-beta2 and the holo-beta2 forms consist of two domains, (N domain, C domain). The pyridoxal 5'-phosphate-bound holo-form has multiple interactions between the two domains and a long loop (residues 260-310), which are missing in the apo-form	Escherichia coli

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Release 2023.1 (January 2023)