SCIENCE@home

Crystal Structures of Threonine Synthase from Thermus thermophilus HB8

R. Omi,M. Goto,I. Miyahara,H. Mizuguchi,H. Hayashi,H. Kagamiyama,K. Hirotsu

Published 2003 in Journal of Biological Chemistry

ABSTRACT

Threonine synthase, which is a PLP-dependent enzyme, catalyzes the β,γ-replacement reaction of l-homoserine phosphate to yield threonine and inorganic phosphate. The three-dimensional structures of the enzyme from Thermus thermophilus HB8 in its unliganded form and complexed with the substrate analogue 2-amino-5-phosphonopentanoic acid have been determined at 2.15 and 2.0 Å resolution, respectively. The complexed form, assigned as an enamine, uncovered the interactions of the cofactor-analogue conjugate with the active site residues. The binding of the substrate analogue induces a large conformational change at the domain level. The small domain rotates by about 25° and approaches the large domain to close the active site. The complicated catalytic process of the enzyme has been elucidated based on the complex structure to reveal the stereochemistry of the reaction and to present the released inorganic phosphate as a possible catalyst to carry a proton to the Cγ atom of the substrate.

PUBLICATION RECORD

CITATION MAP

EXTRACTION MAP

CLAIMS

  • No claims are published for this paper.

CONCEPTS

  • No concepts are published for this paper.

REFERENCES

Showing 1-43 of 43 references · Page 1 of 1

CITED BY

Showing 1-36 of 36 citing papers · Page 1 of 1