1uim
From Proteopedia
(New page: 200px<br /><applet load="1uim" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uim, resolution 2.15Å" /> '''Crystal Structure of...) |
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| - | [[Image:1uim.jpg|left|200px]]<br /><applet load="1uim" size=" | + | [[Image:1uim.jpg|left|200px]]<br /><applet load="1uim" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uim, resolution 2.15Å" /> | caption="1uim, resolution 2.15Å" /> | ||
'''Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Orthorhombic Crystal Form'''<br /> | '''Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Orthorhombic Crystal Form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Threonine synthase, which is a PLP-dependent enzyme, catalyzes the | + | 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== | ==About this Structure== | ||
| - | 1UIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Threonine_synthase Threonine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.1 4.2.3.1] Full crystallographic information is available from [http:// | + | 1UIM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Threonine_synthase Threonine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.1 4.2.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UIM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Threonine synthase]] | [[Category: Threonine synthase]] | ||
[[Category: Omi, R.]] | [[Category: Omi, R.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: PLP]] | [[Category: PLP]] | ||
[[Category: plp-dependent enzyme]] | [[Category: plp-dependent enzyme]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:56 2008'' |
Revision as of 13:24, 21 February 2008
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Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Orthorhombic Crystal Form
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
1UIM is a Single protein structure of sequence from Thermus thermophilus with as ligand. 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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