7VG5
10,5-methenyltetrahydrofolate cyclohydrolase from Methylobacterium extorquens AM1 with tetrahydrofolate
Summary for 7VG5
| Entry DOI | 10.2210/pdb7vg5/pdb |
| Descriptor | Methenyltetrahydrofolate cyclohydrolase, (6S)-5,6,7,8-TETRAHYDROFOLATE (3 entities in total) |
| Functional Keywords | methylobacterium extorquens am1, tetrahydrofolate cycle, formate assimilation, 5, 10-methenyltetrahydrofolate cyclohydrolase, hydrolase |
| Biological source | Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) |
| Total number of polymer chains | 2 |
| Total formula weight | 46524.79 |
| Authors | Kim, S.,Lee, S.,Kim, I.-K.,Seo, H.,Kim, K.-J. (deposition date: 2021-09-14, release date: 2022-07-06, Last modification date: 2023-11-29) |
| Primary citation | Kim, S.,Lee, S.H.,Kim, I.K.,Seo, H.,Kim, K.J. Structural insight into a molecular mechanism of methenyltetrahydrofolate cyclohydrolase from Methylobacterium extorquens AM1. Int.J.Biol.Macromol., 202:234-240, 2022 Cited by PubMed Abstract: Bioconversion of the C1 compounds into value-added products is one of the CO-reducing strategies. In particular, because CO can be easily converted into formate, the efficient and direct bioconversion of CO through formate assimilation is attracting attention. The tetrahydrofolate (THF) cycle is the highly efficient reconstructed formate assimilation pathway, and 5,10-methenyltetrahydrofolate cyclohydrolase (FchA) is an essential enzyme involved in the THF cycle. In this study, a kinetic analysis of FchA from Methylobacterium extorquens AM1 (MeFchA) was performed and revealed that the enzyme has much higher cyclization than hydrolyzation activity, making it an optimal enzyme for formate assimilation. The crystal structure of MeFchA in the apo- and the THF-complexed forms was also determined, revealing that the substrate-binding site of the enzyme has three differently charged regions to stabilize the three differently charged moieties of the formyl-THF substrate. The residues involved in the substrate binding were also verified through site-directed mutagenesis. This study provides a biochemical and structural basis for the molecular mechanism underlying formate assimilation. PubMed: 35051495DOI: 10.1016/j.ijbiomac.2022.01.072 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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