1v7c
From Proteopedia
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Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue
Overview
Threonine synthase, which is a PLP-dependent enzyme, catalyzes the, beta,gamma-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 A 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 degrees 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 Cgamma atom of, the substrate.
About this Structure
1V7C is a Single protein structure of sequence from Thermus thermophilus with HEY as ligand. This structure superseeds the now removed PDB entry 1UIQ. Active as Threonine synthase, with EC number 4.2.3.1 Full crystallographic information is available from OCA.
Reference
Crystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism., Omi R, Goto M, Miyahara I, Mizuguchi H, Hayashi H, Kagamiyama H, Hirotsu K, J Biol Chem. 2003 Nov 14;278(46):46035-45. Epub 2003 Sep 2. PMID:12952961
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