1v7c

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[[Image:1v7c.jpg|left|200px]]<br /><applet load="1v7c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v7c.jpg|left|200px]]
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caption="1v7c, resolution 2.00&Aring;" />
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'''Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue'''<br />
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{{Structure
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|PDB= 1v7c |SIZE=350|CAPTION= <scene name='initialview01'>1v7c</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HEY:(2E)-2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]-5-PHOSPHONOPENT-2-ENOIC ACID'>HEY</scene>
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|ACTIVITY= [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]
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|GENE= HB8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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}}
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'''Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1V7C 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=HEY:'>HEY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1UIQ. 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=1V7C OCA].
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1V7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. This structure supersedes the now removed PDB entry 1UIQ. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7C OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12952961 12952961]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12952961 12952961]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:41:46 2008''

Revision as of 12:41, 20 March 2008


PDB ID 1v7c

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Gene: HB8 (Thermus thermophilus)
Activity: Threonine synthase, with EC number 4.2.3.1
Coordinates: save as pdb, mmCIF, xml



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. This structure supersedes the now removed PDB entry 1UIQ. 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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