2qrk: Difference between revisions
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'''Crystal Structure of AMP-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae''' | '''Crystal Structure of AMP-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae''' | ||
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Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae., Andi B, Xu H, Cook PF, West AH, Biochemistry. 2007 Nov 6;46(44):12512-21. Epub 2007 Oct 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17939687 17939687] | Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae., Andi B, Xu H, Cook PF, West AH, Biochemistry. 2007 Nov 6;46(44):12512-21. Epub 2007 Oct 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17939687 17939687] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Andi, B.]] | [[Category: Andi, B.]] | ||
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[[Category: West, A H.]] | [[Category: West, A H.]] | ||
[[Category: Xu, H.]] | [[Category: Xu, H.]] | ||
[[Category: | [[Category: Acetylation]] | ||
[[Category: | [[Category: Alpha-aminoadipate pathway]] | ||
[[Category: | [[Category: Amino-acid biosynthesis]] | ||
[[Category: | [[Category: Amp]] | ||
[[Category: | [[Category: Cytoplasm]] | ||
[[Category: | [[Category: Fungal lysine biosynthesis]] | ||
[[Category: | [[Category: Nad]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: | [[Category: Rossmann fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:32:27 2008'' | |||
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Revision as of 15:32, 4 May 2008
Crystal Structure of AMP-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae
OverviewOverview
Three structures of saccharopine dehydrogenase (l-lysine-forming) (SDH) have been determined in the presence of sulfate, adenosine monophosphate (AMP), and oxalylglycine (OxGly). In the sulfate-bound structure, a sulfate ion binds in a cleft between the two domains of SDH, occupies one of the substrate carboxylate binding sites, and results in partial closure of the active site of the enzyme due to a domain rotation of almost 12 degrees in comparison to the apoenzyme structure. In the second structure, AMP binds to the active site in an area where the NAD+ cofactor is expected to bind. All of the AMP moieties (adenine ring, ribose, and phosphate) interact with specific residues of the enzyme. In the OxGly-bound structure, carboxylates of OxGly interact with arginine residues representative of the manner in which substrate (alpha-ketoglutarate and saccharopine) may bind. The alpha-keto group of OxGly interacts with Lys77 and His96, which are candidates for acid-base catalysis. Analysis of ligand-enzyme interactions, comparative structural analysis, corroboration with kinetic data, and discussion of a ternary complex model are presented in this study.
About this StructureAbout this Structure
2QRK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of ligand-bound saccharopine dehydrogenase from Saccharomyces cerevisiae., Andi B, Xu H, Cook PF, West AH, Biochemistry. 2007 Nov 6;46(44):12512-21. Epub 2007 Oct 16. PMID:17939687 Page seeded by OCA on Sun May 4 15:32:27 2008