2axq

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[[Image:2axq.gif|left|200px]]<br /><applet load="2axq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2axq.gif|left|200px]]
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caption="2axq, resolution 1.700&Aring;" />
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'''Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae'''<br />
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{{Structure
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|PDB= 2axq |SIZE=350|CAPTION= <scene name='initialview01'>2axq</scene>, resolution 1.700&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Saccharopine_dehydrogenase_(NADP(+),_L-glutamate-forming) Saccharopine dehydrogenase (NADP(+), L-glutamate-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.10 1.5.1.10]
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|GENE= LYS9, LYS13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AXQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Saccharopine_dehydrogenase_(NADP(+),_L-glutamate-forming) Saccharopine dehydrogenase (NADP(+), L-glutamate-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.10 1.5.1.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXQ OCA].
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2AXQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXQ OCA].
==Reference==
==Reference==
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Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution., Andi B, Cook PF, West AH, Cell Biochem Biophys. 2006;46(1):17-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16943620 16943620]
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Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution., Andi B, Cook PF, West AH, Cell Biochem Biophys. 2006;46(1):17-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16943620 16943620]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharopine dehydrogenase (NADP(+), L-glutamate-forming)]]
[[Category: Saccharopine dehydrogenase (NADP(+), L-glutamate-forming)]]
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[[Category: saccharopine reductase fold (domain ii)]]
[[Category: saccharopine reductase fold (domain ii)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:55:09 2008''

Revision as of 13:55, 20 March 2008


PDB ID 2axq

Drag the structure with the mouse to rotate
, resolution 1.700Å
Ligands:
Gene: LYS9, LYS13 (Saccharomyces cerevisiae)
Activity: Saccharopine dehydrogenase (NADP(+), L-glutamate-forming), with EC number 1.5.1.10
Coordinates: save as pdb, mmCIF, xml



Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae


Overview

The three-dimensional structure of the saccharopine reductase enzyme from the budding yeast Saccharomyces cerevisiae was determined to 1.7-A resolution in the apo form by using molecular replacement. The enzyme monomer consists of three domains: domain I is a variant of the Rossmann fold, domain II folds into a alpha/beta structure containing a mixed seven-stranded beta-sheet as the central core, and domain III has an all-helical fold. Comparative fold alignment with the enzyme from Magnaporthe grisea suggests that domain I binds to NADPH, and domain II binds to saccharopine and is involved in dimer formation. Domain III is involved in closing the active site of the enzyme once substrates are bound. Structural comparison of the saccharopine reductase enzymes from S. cerevisiae and M. grisea indicates that domain II has the highest number of conserved residues, suggesting that it plays an important role in substrate binding and in spatially orienting domains I and III.

About this Structure

2AXQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the his-tagged saccharopine reductase from Saccharomyces cerevisiae at 1.7-A resolution., Andi B, Cook PF, West AH, Cell Biochem Biophys. 2006;46(1):17-26. PMID:16943620

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