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2qrl
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=OGA:N-OXALYOLGLYCINE'>OGA</scene> | |LIGAND= <scene name='pdbligand=OGA:N-OXALYOLGLYCINE'>OGA</scene> | ||
| - | |ACTIVITY= [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] | + | |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> |
|GENE= LYS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= LYS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2q99|2Q99]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qrl OCA], [http://www.ebi.ac.uk/pdbsum/2qrl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qrl RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: West, A H.]] | [[Category: West, A H.]] | ||
[[Category: Xu, H.]] | [[Category: Xu, H.]] | ||
| - | [[Category: OGA]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: alpha-aminoadipate pathway]] | [[Category: alpha-aminoadipate pathway]] | ||
| Line 38: | Line 40: | ||
[[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 Mon Mar 31 04:52:30 2008'' |
Revision as of 01:52, 31 March 2008
| |||||||
| , resolution 1.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | LYS1 (Saccharomyces cerevisiae) | ||||||
| Activity: | Saccharopine dehydrogenase (NAD(+), L-lysine-forming), with EC number 1.5.1.7 | ||||||
| Related: | 2Q99
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mon Mar 31 04:52:30 2008
Categories: Saccharomyces cerevisiae | Saccharopine dehydrogenase (NAD(+), L-lysine-forming) | Single protein | Andi, B. | Cook, P F. | West, A H. | Xu, H. | Acetylation | Alpha-aminoadipate pathway | Amino-acid biosynthesis | Cytoplasm | Fungal lysine biosynthesis | Nad | Oxalylglycine | Oxidoreductase | Rossmann fold
