2qrl

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spinqualitylabelsall models 2qrl, resolution 1.600Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

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