2axq

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[[Image:2axq.gif|left|200px]]
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{{STRUCTURE_2axq| PDB=2axq | SCENE= }}
{{STRUCTURE_2axq| PDB=2axq | SCENE= }}
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'''Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae'''
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===Apo histidine-tagged saccharopine dehydrogenase (L-Glu forming) from Saccharomyces cerevisiae===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_16943620}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16943620 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16943620}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16943620 16943620]
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]
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Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis., Johansson E, Steffens JJ, Lindqvist Y, Schneider G, Structure. 2000 Oct 15;8(10):1037-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080625 11080625]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fungal lysine biosynthesis]]
[[Category: Fungal lysine biosynthesis]]
[[Category: Rossmann fold variant]]
[[Category: Rossmann fold variant]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:36:50 2008''

Revision as of 12:36, 28 July 2008

Image:2axq.png

Template:STRUCTURE 2axq

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

Template:ABSTRACT PUBMED 16943620

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

Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis., Johansson E, Steffens JJ, Lindqvist Y, Schneider G, Structure. 2000 Oct 15;8(10):1037-47. PMID:11080625

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