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2qrl
From Proteopedia
(New page: 200px<br /><applet load="2qrl" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qrl, resolution 1.600Å" /> '''Crystal Structure o...) |
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==Overview== | ==Overview== | ||
| - | Three structures of saccharopine dehydrogenase (l-lysine-forming) (SDH) | + | 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 Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal | + | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17939687 17939687] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Saccharopine dehydrogenase (NAD(+), L-lysine-forming)]] | [[Category: Saccharopine dehydrogenase (NAD(+), L-lysine-forming)]] | ||
[[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: Xu, H.]] | [[Category: Xu, H.]] | ||
[[Category: OGA]] | [[Category: OGA]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:42 2008'' |
Revision as of 16:41, 21 February 2008
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Crystal Structure of Oxalylglycine-bound Saccharopine Dehydrogenase (L-Lys Forming) from Saccharomyces cerevisiae
Overview
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 Structure
2QRL is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Saccharopine dehydrogenase (NAD(+), L-lysine-forming), with EC number 1.5.1.7 Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 18:41:42 2008
Categories: Saccharomyces cerevisiae | Saccharopine dehydrogenase (NAD(+), L-lysine-forming) | Single protein | Andi, B. | Cook, P F. | West, A H. | Xu, H. | OGA | Acetylation | Alpha-aminoadipate pathway | Amino-acid biosynthesis | Cytoplasm | Fungal lysine biosynthesis | Nad | Oxalylglycine | Oxidoreductase | Rossmann fold
