Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii. Issue 8 (4th August 2016)

• Record Type: Journal Article
• Authors: Watanabe, Yuzo; Yanai, Hisaaki; Kanagawa, Mayumi; Suzuki, Sakiko; Tamura, Satoko; Okada, Kiyoshi; Baba, Seiki; Kumasaka, Takashi; Agari, Yoshihiro; Chen, Lirong; Fu, Zheng-Qing; Chrzas, John; Wang, Bi-Cheng; Nakagawa, Noriko; Ebihara, Akio; Masui, Ryoji; Kuramitsu, Seiki; Yokoyama, Shigeyuki; Sampei, Gen-ichi; Kawai, Gota
• Is Part Of: Acta crystallographica. Volume 72:Issue 8(2016:Aug.)
• Page Start: 627
• Page End: 635
• Publication Date: 2016-08-04
• Subjects: purine nucleotide‐biosynthetic pathway -- formylglycinamide ribonucleotide amidotransferase -- PurS -- crystal structure -- Thermus thermophilus -- Sulfolobus tokodaii -- Methanocaldococcus jannaschii; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1600978X
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from T. thermophilus, S. tokodaii and M. jannaschii are determined and their structural characteristics are analyzed. Abstract : The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii were determined and their structural characteristics were analyzed. For PurS from T. thermophilus, two structures were determined using two crystals that were grown in different conditions. The four structures in the dimeric form were almost identical to one another despite their relatively low sequence identities. This is also true for all PurS structures determined to date. A few residues were conserved among PurSs and these are located at the interaction site with PurL and PurQ, the other subunits of the formylglycinamide ribonucleotide amidotransferase. Molecular‐dynamics simulations of the PurS dimer as well as a model of the complex of the PurS dimer, PurL and PurQ suggest that PurS plays some role in the catalysis of the enzyme by its bending motion.