3NL9

Crystal structure of a putative NTP pyrophosphohydrolase (Exig_1061) from EXIGUOBACTERIUM SP. 255-15 at 1.78 A resolution

「3MQU」から置き換えられました 「2RFP」から置き換えられました

3NL9 の概要

• エントリーDOI: 10.2210/pdb3nl9/pdb
• 分子名称: putative NTP pyrophosphohydrolase, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, hydrolase
• 由来する生物種: Exiguobacterium sibiricum 255-15 (Exiguobacterium sp. 255-15)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19521.20

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2010-06-21, 公開日: 2010-07-21, 最終更新日: 2024-10-09)

主引用文献

Han, G.W.,Elsliger, M.A.,Yeates, T.O.,Xu, Q.,Murzin, A.G.,Krishna, S.S.,Jaroszewski, L.,Abdubek, P.,Astakhova, T.,Axelrod, H.L.,Carlton, D.,Chen, C.,Chiu, H.J.,Clayton, T.,Das, D.,Deller, M.C.,Duan, L.,Ernst, D.,Feuerhelm, J.,Grant, J.C.,Grzechnik, A.,Jin, K.K.,Johnson, H.A.,Klock, H.E.,Knuth, M.W.,Kozbial, P.,Kumar, A.,Lam, W.W.,Marciano, D.,McMullan, D.,Miller, M.D.,Morse, A.T.,Nigoghossian, E.,Okach, L.,Reyes, R.,Rife, C.L.,Sefcovic, N.,Tien, H.J.,Trame, C.B.,van den Bedem, H.,Weekes, D.,Hodgson, K.O.,Wooley, J.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.
Structure of a putative NTP pyrophosphohydrolase: YP_001813558.1 from Exiguobacterium sibiricum 255-15.
Acta Crystallogr.,Sect.F, 66:1237-1244, 2010

PubMed Abstract: The crystal structure of a putative NTPase, YP_001813558.1 from Exiguobacterium sibiricum 255-15 (PF09934, DUF2166) was determined to 1.78 Å resolution. YP_001813558.1 and its homologs (dimeric dUTPases, MazG proteins and HisE-encoded phosphoribosyl ATP pyrophosphohydrolases) form a superfamily of all-α-helical NTP pyrophosphatases. In dimeric dUTPase-like proteins, a central four-helix bundle forms the active site. However, in YP_001813558.1, an unexpected intertwined swapping of two of the helices that compose the conserved helix bundle results in a `linked dimer' that has not previously been observed for this family. Interestingly, despite this novel mode of dimerization, the metal-binding site for divalent cations, such as magnesium, that are essential for NTPase activity is still conserved. Furthermore, the active-site residues that are involved in sugar binding of the NTPs are also conserved when compared with other α-helical NTPases, but those that recognize the nucleotide bases are not conserved, suggesting a different substrate specificity.

PubMed: 20944217
DOI: 10.1107/S1744309110025534

実験手法

X-RAY DIFFRACTION (1.78 Å)