3VPD

LysX from Thermus thermophilus complexed with AMP-PNP

Summary for 3VPD

• Entry DOI: 10.2210/pdb3vpd/pdb
• Related: 3VPB 3VPC
• Descriptor: Ribosomal protein S6 modification protein, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, butanoic acid, ... (5 entities in total)
• Functional Keywords: atp-dependenet amine/thiol ligase family, atp-dependenet amine/thiol ligase, ligase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 63027.74

Authors

Tomita, T.,Ouchi, T.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2012-02-29, release date: 2013-02-27, Last modification date: 2023-11-08)

Primary citation

Ouchi, T.,Tomita, T.,Horie, A.,Yoshida, A.,Takahashi, K.,Nishida, H.,Lassak, K.,Taka, H.,Mineki, R.,Fujimura, T.,Kosono, S.,Nishiyama, C.,Masui, R.,Kuramitsu, S.,Albers, S.V.,Kuzuyama, T.,Nishiyama, M.
Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
Nat.Chem.Biol., 9:277-283, 2013

PubMed Abstract: LysW has been identified as a carrier protein in the lysine biosynthetic pathway that is active through the conversion of α-aminoadipate (AAA) to lysine. In this study, we found that the hyperthermophilic archaeon, Sulfolobus acidocaldarius, not only biosynthesizes lysine through LysW-mediated protection of AAA but also uses LysW to protect the amino group of glutamate in arginine biosynthesis. In this archaeon, after LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. The crystal structure of ArgX, the enzyme responsible for modification and protection of the amino moiety of glutamate with LysW, was determined in complex with LysW. Structural comparison and enzymatic characterization using Sulfolobus LysX, Sulfolobus ArgX and Thermus LysX identify the amino acid motif responsible for substrate discrimination between AAA and glutamate. Phylogenetic analysis reveals that gene duplication events at different stages of evolution led to ArgX and LysX.

PubMed: 23434852
DOI: 10.1038/nchembio.1200

Experimental method

X-RAY DIFFRACTION (1.95 Å)