7OWJ

Odinarchaeota Adenylate kinase (OdinAK) in complex with GTP

7OWJ の概要

• エントリーDOI: 10.2210/pdb7owj/pdb
• 分子名称: Adenylate kinase, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: phosphotransferase, odinarchaeota adenylate kinase, asgard group, gtp, transferase
• 由来する生物種: Candidatus Odinarchaeota archaeon LCB_4
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 140440.18

構造登録者

Aberg-Zingmark, E.,Grundstrom, C.,Verma, A.,Wolf-Watz, M.,Sauer, U.H.,Sauer-Eriksson, A.E. (登録日: 2021-06-18, 公開日: 2022-09-28, 最終更新日: 2024-01-31)

主引用文献

Verma, A.,Aberg-Zingmark, E.,Sparrman, T.,Mushtaq, A.U.,Rogne, P.,Grundstrom, C.,Berntsson, R.,Sauer, U.H.,Backman, L.,Nam, K.,Sauer-Eriksson, E.,Wolf-Watz, M.
Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases.
Sci Adv, 8:eabm4089-eabm4089, 2022

PubMed Abstract: Enzymatic catalysis is critically dependent on selectivity, active site architecture, and dynamics. To contribute insights into the interplay of these properties, we established an approach with NMR, crystallography, and MD simulations focused on the ubiquitous phosphotransferase adenylate kinase (AK) isolated from (OdinAK). belongs to the Asgard archaeal phylum that is believed to be the closest known ancestor to eukaryotes. We show that OdinAK is a hyperthermophilic trimer that, contrary to other AK family members, can use all NTPs for its phosphorylation reaction. Crystallographic structures of OdinAK-NTP complexes revealed a universal NTP-binding motif, while F NMR experiments uncovered a conserved and rate-limiting dynamic signature. As a consequence of trimerization, the active site of OdinAK was found to be lacking a critical catalytic residue and is therefore considered to be "atypical." On the basis of discovered relationships with human monomeric homologs, our findings are discussed in terms of evolution of enzymatic substrate specificity and cold adaptation.

PubMed: 36332013
DOI: 10.1126/sciadv.abm4089

実験手法

X-RAY DIFFRACTION (2.5 Å)