3AUF

Crystal structure of glycinamide ribonucleotide transformylase 1 from Symbiobacterium toebii

3AUF の概要

• エントリーDOI: 10.2210/pdb3auf/pdb
• 分子名称: Glycinamide ribonucleotide transformylase 1 (2 entities in total)
• 機能のキーワード: structural genomics, riken structural genomics/proteomics initiative, rsgi, rossmann fold, transformylase, folate binding, transferase
• 由来する生物種: Symbiobacterium toebii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25045.76

構造登録者

Kanagawa, M.,Baba, S.,Nagira, T.,Kuramitsu, S.,Yokoyama, S.,Sampei, G.,Kawai, G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2011-02-03, 公開日: 2012-03-07, 最終更新日: 2023-11-01)

主引用文献

Sampei, G.,Kanagawa, M.,Baba, S.,Shimasaki, T.,Taka, H.,Mitsui, S.,Fujiwara, S.,Yanagida, Y.,Kusano, M.,Suzuki, S.,Terao, K.,Kawai, H.,Fukai, Y.,Nakagawa, N.,Ebihara, A.,Kuramitsu, S.,Yokoyama, S.,Kawai, G.
Structures and reaction mechanisms of the two related enzymes, PurN and PurU.
J.Biochem., 154:569-579, 2013

PubMed Abstract: The crystal structures of glycinamide ribonucleotide transformylases (PurNs) from Aquifex aeolicus (Aa), Geobacillus kaustophilus (Gk) and Symbiobacterium toebii (St), and of formyltetrahydrofolate hydrolase (PurU) from Thermus thermophilus (Tt) were determined. The monomer structures of the determined PurN and PurU were very similar to the known structure of PurN, but oligomeric states were different; AaPurN and StPurN formed dimers, GkPurN formed monomer and PurU formed tetramer in the crystals. PurU had a regulatory ACT domain in its N-terminal side. So far several structures of PurUs have been determined, yet, the mechanisms of the catalysis and the regulation of PurU have not been elucidated. We, therefore, modelled ligand-bound structures of PurN and PurU, and performed molecular dynamics simulations to elucidate the reaction mechanisms. The evolutionary relationship of the two enzymes is discussed based on the comparisons of the structures and the catalytic mechanisms.

PubMed: 24108189
DOI: 10.1093/jb/mvt090

実験手法

X-RAY DIFFRACTION (2.07 Å)