2q99: Difference between revisions

Revision as of 14:33, 4 May 2008

Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae

OverviewOverview

The 1.64 A structure of the apoenzyme form of saccharopine dehydrogenase (SDH) from Saccharomyces cerevisiae shows the enzyme to be composed of two domains with similar dinucleotide binding folds with a deep cleft at the interface. The structure reveals homology to alanine dehydrogenase, despite low primary sequence similarity. A model of the ternary complex of SDH, NAD, and saccharopine identifies residues Lys77 and Glu122 as potentially important for substrate binding and/or catalysis, consistent with a proton shuttle mechanism. Furthermore, the model suggests that a conformational change is required for catalysis and that residues Lys99 and Asp281 may be instrumental in mediating this change. Analysis of the crystal structure in the context of other homologous enzymes from pathogenic fungi and human sources sheds light into the suitability of SDH as a target for antimicrobial drug development.

About this StructureAbout this Structure

2Q99 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae., Burk DL, Hwang J, Kwok E, Marrone L, Goodfellow V, Dmitrienko GI, Berghuis AM, J Mol Biol. 2007 Oct 26;373(3):745-54. Epub 2007 Aug 24. PMID:17854830 Page seeded by OCA on Sun May 4 14:33:55 2008

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OCA

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 [[Image:2q99.jpg|left|200px]]
- {{Structure
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-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Saccharopine_dehydrogenase_(NAD(+),_L-lysine-forming) Saccharopine dehydrogenase (NAD(+), L-lysine-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.7 1.5.1.7] </span>
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-|GENE= LYS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q99 OCA], [http://www.ebi.ac.uk/pdbsum/2q99 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q99 RCSB]</span>
-}}
 '''Crystal Structure of Saccharopine Dehydrogenase from Saccharomyces cerevisiae'''
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 Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae., Burk DL, Hwang J, Kwok E, Marrone L, Goodfellow V, Dmitrienko GI, Berghuis AM, J Mol Biol. 2007 Oct 26;373(3):745-54. Epub 2007 Aug 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17854830 17854830]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Saccharopine dehydrogenase (NAD(+), L-lysine-forming)]]
 [[Category: Single protein]]
 [[Category: Berghuis, A M.]]
 [[Category: Burk, D L.]]
-[[Category: alpha-aminoadipate pathway]]
+[[Category: Alpha-aminoadipate pathway]]
-[[Category: alpha/beta protein]]
+[[Category: Alpha/beta protein]]
-[[Category: dehydrogenase]]
+[[Category: Dehydrogenase]]
-[[Category: fungal lysine synthesis]]
+[[Category: Fungal lysine synthesis]]
-[[Category: oxidoreductase]]
+[[Category: Oxidoreductase]]
-[[Category: rossmann fold]]
+[[Category: Rossmann fold]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 14:33:55 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:46:33 2008''