| Structural highlights
Function
[LYSX_THET8] Catalyzes the ATP-dependent formation of a covalent bond between the amino group of alpha-aminoadipate (AAA) and the gamma-carboxyl group of the C-terminal glutamate residue in LysW.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The thermophilic bacterium Thermus thermophilus synthesizes lysine through the alpha-aminoadipate pathway, which uses alpha-aminoadipate as a biosynthetic intermediate of lysine. LysX is the essential enzyme in this pathway, and is believed to catalyze the acylation of alpha-aminoadipate. We have determined the crystal structures of LysX and its complex with ADP at 2.0A and 2.38A resolutions, respectively. LysX is composed of three alpha+beta domains, each composed of a four to five-stranded beta-sheet core flanked by alpha-helices. The C-terminal and central domains form an ATP-grasp fold, which is responsible for ATP binding. LysX has two flexible loop regions, which are expected to play an important role in substrate binding and protection. In spite of the low level of sequence identity, the overall fold of LysX is surprisingly similar to that of other ATP-grasp fold proteins, such as D-Ala:D-Ala ligase, PurT-encoded glycinamide ribonucleotide transformylase, glutathione synthetase, and synapsin I. In particular, they share a similar spatial arrangement of the amino acid residues around the ATP-binding site. This observation strongly suggests that LysX is an ATP-utilizing enzyme that shares a common evolutionary ancestor with other ATP-grasp fold proteins possessing a carboxylate-amine/thiol ligase activity.
Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8.,Sakai H, Vassylyeva MN, Matsuura T, Sekine S, Gotoh K, Nishiyama M, Terada T, Shirouzu M, Kuramitsu S, Vassylyev DG, Yokoyama S J Mol Biol. 2003 Sep 19;332(3):729-40. PMID:12963379[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Horie A, Tomita T, Saiki A, Kono H, Taka H, Mineki R, Fujimura T, Nishiyama C, Kuzuyama T, Nishiyama M. Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus. Nat Chem Biol. 2009 Sep;5(9):673-9. doi: 10.1038/nchembio.198. Epub 2009 Jul 20. PMID:19620981 doi:http://dx.doi.org/10.1038/nchembio.198
- ↑ Sakai H, Vassylyeva MN, Matsuura T, Sekine S, Gotoh K, Nishiyama M, Terada T, Shirouzu M, Kuramitsu S, Vassylyev DG, Yokoyama S. Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8. J Mol Biol. 2003 Sep 19;332(3):729-40. PMID:12963379
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