3W7B
Crystal structure of formyltetrahydrofolate deformylase from Thermus thermophilus HB8
Summary for 3W7B
| Entry DOI | 10.2210/pdb3w7b/pdb |
| Descriptor | Formyltetrahydrofolate deformylase (2 entities in total) |
| Functional Keywords | formyltetrahydrofolate deformylase, formyltetrahydrofolate, hydrolase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 65675.58 |
| Authors | Sampei, G.,Yanagida, Y.,Ogata, N.,Kusano, M.,Terao, K.,Kawai, H.,Fukai, Y.,Kanagawa, M.,Inoue, Y.,Baba, S.,Kawai, G. (deposition date: 2013-02-28, release date: 2014-01-08, Last modification date: 2023-11-08) |
| Primary citation | 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 Cited by 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: 24108189DOI: 10.1093/jb/mvt090 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.71 Å) |
Structure validation
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