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Conformational Changes in the tryptophan synthase from a hyperthermophile upon alpha2beta2 complex formation: crystal structure of the complex.
Biochemistry. 2005 Aug 30; 44(34):11417-27.B

Abstract

The three-dimensional structure of the bifunctional tryptophan synthase alpha(2)beta(2) complex from Pyrococcus furiosus was determined by crystallographic analysis. This crystal structure, with the structures of an alpha subunit monomer and a beta(2) subunit dimer that have already been reported, is the first structural set in which changes in structure that occur upon the association of the individual tryptophan synthase subunits were observed. To elucidate the structural basis of the stimulation of the enzymatic activity of each of the alpha and beta(2) subunits upon alpha(2)beta(2) complex formation, the conformational changes due to complex formation were analyzed in detail compared with the structures of the alpha monomer and beta(2) subunit dimer. The major conformational changes due to complex formation occurred in the region correlated with the catalytic function of the enzyme as follows. (1) Structural changes in the beta subunit were greater than those in the alpha subunit. (2) Large movements of A46 and L165 in the alpha subunit due to complex formation caused a more open conformation favoring the entry of the substrate at the alpha active site. (3) The major changes in the beta subunit were the broadening of a long tunnel through which the alpha subunit product (indole) is transferred to the beta active site and the opening of an entrance at the beta active site. (4) The changes in the conformations of both the alpha and beta subunits due to complex formation contributed to the stabilization of the subunit association, which is critical for the stimulation of the enzymatic activities.

Authors+Show Affiliations

Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16114878

Citation

Lee, Soo Jae, et al. "Conformational Changes in the Tryptophan Synthase From a Hyperthermophile Upon Alpha2beta2 Complex Formation: Crystal Structure of the Complex." Biochemistry, vol. 44, no. 34, 2005, pp. 11417-27.
Lee SJ, Ogasahara K, Ma J, et al. Conformational Changes in the tryptophan synthase from a hyperthermophile upon alpha2beta2 complex formation: crystal structure of the complex. Biochemistry. 2005;44(34):11417-27.
Lee, S. J., Ogasahara, K., Ma, J., Nishio, K., Ishida, M., Yamagata, Y., Tsukihara, T., & Yutani, K. (2005). Conformational Changes in the tryptophan synthase from a hyperthermophile upon alpha2beta2 complex formation: crystal structure of the complex. Biochemistry, 44(34), 11417-27.
Lee SJ, et al. Conformational Changes in the Tryptophan Synthase From a Hyperthermophile Upon Alpha2beta2 Complex Formation: Crystal Structure of the Complex. Biochemistry. 2005 Aug 30;44(34):11417-27. PubMed PMID: 16114878.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Conformational Changes in the tryptophan synthase from a hyperthermophile upon alpha2beta2 complex formation: crystal structure of the complex. AU - Lee,Soo Jae, AU - Ogasahara,Kyoko, AU - Ma,Jichun, AU - Nishio,Kazuya, AU - Ishida,Masami, AU - Yamagata,Yuriko, AU - Tsukihara,Tomitake, AU - Yutani,Katsuhide, PY - 2005/8/24/pubmed PY - 2005/11/3/medline PY - 2005/8/24/entrez SP - 11417 EP - 27 JF - Biochemistry JO - Biochemistry VL - 44 IS - 34 N2 - The three-dimensional structure of the bifunctional tryptophan synthase alpha(2)beta(2) complex from Pyrococcus furiosus was determined by crystallographic analysis. This crystal structure, with the structures of an alpha subunit monomer and a beta(2) subunit dimer that have already been reported, is the first structural set in which changes in structure that occur upon the association of the individual tryptophan synthase subunits were observed. To elucidate the structural basis of the stimulation of the enzymatic activity of each of the alpha and beta(2) subunits upon alpha(2)beta(2) complex formation, the conformational changes due to complex formation were analyzed in detail compared with the structures of the alpha monomer and beta(2) subunit dimer. The major conformational changes due to complex formation occurred in the region correlated with the catalytic function of the enzyme as follows. (1) Structural changes in the beta subunit were greater than those in the alpha subunit. (2) Large movements of A46 and L165 in the alpha subunit due to complex formation caused a more open conformation favoring the entry of the substrate at the alpha active site. (3) The major changes in the beta subunit were the broadening of a long tunnel through which the alpha subunit product (indole) is transferred to the beta active site and the opening of an entrance at the beta active site. (4) The changes in the conformations of both the alpha and beta subunits due to complex formation contributed to the stabilization of the subunit association, which is critical for the stimulation of the enzymatic activities. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/16114878/Conformational_Changes_in_the_tryptophan_synthase_from_a_hyperthermophile_upon_alpha2beta2_complex_formation:_crystal_structure_of_the_complex_ DB - PRIME DP - Unbound Medicine ER -