2zg5
From Proteopedia
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|PDB= 2zg5 |SIZE=350|CAPTION= <scene name='initialview01'>2zg5</scene>, resolution 2.26Å | |PDB= 2zg5 |SIZE=350|CAPTION= <scene name='initialview01'>2zg5</scene>, resolution 2.26Å | ||
|SITE= <scene name='pdbsite=AC1:LEU+Binding+Site+For+Residue+A+398'>AC1</scene>, <scene name='pdbsite=AC2:LEU+Binding+Site+For+Residue+C+398'>AC2</scene> and <scene name='pdbsite=AC3:LEU+Binding+Site+For+Residue+E+398'>AC3</scene> | |SITE= <scene name='pdbsite=AC1:LEU+Binding+Site+For+Residue+A+398'>AC1</scene>, <scene name='pdbsite=AC2:LEU+Binding+Site+For+Residue+C+398'>AC2</scene> and <scene name='pdbsite=AC3:LEU+Binding+Site+For+Residue+E+398'>AC3</scene> | ||
| - | |LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene> | + | |LIGAND= <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/2-aminoadipate_transaminase 2-aminoadipate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.39 2.6.1.39] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/2-aminoadipate_transaminase 2-aminoadipate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.39 2.6.1.39] </span> |
|GENE= lysN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | |GENE= lysN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zg5 OCA], [http://www.ebi.ac.uk/pdbsum/2zg5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2zg5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Nishiyama, M.]] | [[Category: Nishiyama, M.]] | ||
[[Category: Tomita, T.]] | [[Category: Tomita, T.]] | ||
| - | [[Category: LEU]] | ||
[[Category: aminotransferase]] | [[Category: aminotransferase]] | ||
[[Category: protein-plp-leucine complex]] | [[Category: protein-plp-leucine complex]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 05:20:52 2008'' |
Revision as of 02:20, 31 March 2008
| |||||||
| , resolution 2.26Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , | ||||||
| Gene: | lysN (Thermus thermophilus) | ||||||
| Activity: | 2-aminoadipate transaminase, with EC number 2.6.1.39 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of LysN, alpha-aminoadipate aminotransferase (Leucine complex), from Thermus thermophilus HB27
Overview
The extremely thermophilic bacterium Thermus thermophilus HB27 synthesizes lysine through alpha-aminoadipate (AAA). In this study, a T. thermophilus gene encoding the enzyme that catalyses transamination of AAA was cloned as a mammalian kynurenine/AAA aminotransferase (Kat2) gene homologue. A T. thermophilus mutant with disruption of the Kat2 homologue required a longer lag phase for growth and showed slower growth in minimal medium. Furthermore, addition of AAA or lysine shortened the lag phase and improved the growth rate. The Kat2 homologue was therefore termed lysN. LysN recognizes not only 2-oxoadipate, an intermediate of lysine biosynthesis, but also 2-oxoisocaproate, 2-oxoisovalerate and 2-oxo-3-methylvalerate, intermediates of leucine, valine and isoleucine biosyntheses, respectively, along with oxaloacetate, a compound in the TCA cycle, as an amino acceptor. These results suggest multiple roles of LysN in several cellular metabolic pathways including lysine and branched-chain amino acid biosyntheses.
About this Structure
2ZG5 is a Single protein structure of sequence from Thermus thermophilus. This structure supersedes the now removed PDB entry 2DTV. Full crystallographic information is available from OCA.
Reference
alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus., Miyazaki T, Miyazaki J, Yamane H, Nishiyama M, Microbiology. 2004 Jul;150(Pt 7):2327-34. PMID:15256574
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