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1uin

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{{STRUCTURE_1uin| PDB=1uin | SCENE= }}
{{STRUCTURE_1uin| PDB=1uin | SCENE= }}
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'''Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Trigonal Crystal Form'''
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===Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Trigonal Crystal Form===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12952961}}
==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:17:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:41:32 2008''

Revision as of 22:41, 27 July 2008

Image:1uin.png

Template:STRUCTURE 1uin

Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Trigonal Crystal Form

Template:ABSTRACT PUBMED 12952961

About this Structure

1UIN is a Single protein structure of sequence from Thermus thermophilus. 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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