3VPC
ArgX from Sulfolobus tokodaii complexed with ADP
Summary for 3VPC
| Entry DOI | 10.2210/pdb3vpc/pdb |
| Related | 3VPB 3VPD |
| Descriptor | Putative acetylornithine deacetylase, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | atp-dependenet amine/thiol ligase family, atp-dependenet amine/thiol ligase, ligase |
| Biological source | Sulfolobus tokodaii |
| Total number of polymer chains | 4 |
| Total formula weight | 127998.44 |
| Authors | Tomita, T.,Horie, A.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2012-02-29, release date: 2013-02-27, Last modification date: 2024-10-30) |
| 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 Cited by 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: 23434852DOI: 10.1038/nchembio.1200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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