2axq
From Proteopedia
(New page: 200px<br /><applet load="2axq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2axq, resolution 1.700Å" /> '''Apo histidine-tagge...) |
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| - | [[Image:2axq.gif|left|200px]]<br /><applet load="2axq" size=" | + | [[Image:2axq.gif|left|200px]]<br /><applet load="2axq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2axq, resolution 1.700Å" /> | caption="2axq, resolution 1.700Å" /> | ||
'''Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae'''<br /> | '''Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the saccharopine reductase enzyme from | + | 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== | ==About this Structure== | ||
| - | 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 SO4 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Andi, B.]] | [[Category: Andi, B.]] | ||
| - | [[Category: Cook, P | + | [[Category: Cook, P F.]] |
| - | [[Category: West, A | + | [[Category: West, A H.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: alpha-aminoadipate pathway]] | [[Category: alpha-aminoadipate pathway]] | ||
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[[Category: saccharopine reductase fold (domain ii)]] | [[Category: saccharopine reductase fold (domain ii)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:05 2008'' |
Revision as of 14:32, 21 February 2008
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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 with as ligand. Active as Saccharopine dehydrogenase (NADP(+), L-glutamate-forming), with EC number 1.5.1.10 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
Page seeded by OCA on Thu Feb 21 16:32:05 2008
Categories: Saccharomyces cerevisiae | Saccharopine dehydrogenase (NADP(+), L-glutamate-forming) | Single protein | Andi, B. | Cook, P F. | West, A H. | SO4 | Alpha-aminoadipate pathway | Alpha/beta protein | Fungal lysine biosynthesis | Rossmann fold variant | Saccharopine reductase fold (domain ii)
