5VOO
Methionine synthase folate-binding domain with methyltetrahydrofolate from Thermus thermophilus HB8
Summary for 5VOO
| Entry DOI | 10.2210/pdb5voo/pdb |
| Related | 5VON 5VOP |
| Descriptor | 5-methyltetrahydrofolate homocysteine S-methyltransferase, 5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID, SODIUM ION, ... (7 entities in total) |
| Functional Keywords | methyltransferase, pterin binding, b12 binding, oxidoreductase, transferase |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
| Total number of polymer chains | 6 |
| Total formula weight | 201458.32 |
| Authors | Koutmos, M.,Yamada, K. (deposition date: 2017-05-03, release date: 2018-01-17, Last modification date: 2023-10-04) |
| Primary citation | Yamada, K.,Koutmos, M. The folate-binding module of Thermus thermophilus cobalamin-dependent methionine synthase displays a distinct variation of the classical TIM barrel: a TIM barrel with a `twist'. Acta Crystallogr D Struct Biol, 74:41-51, 2018 Cited by PubMed Abstract: Methyl transfer between methyltetrahydrofolate and corrinoid molecules is a key reaction in biology that is catalyzed by a number of enzymes in many prokaryotic and eukaryotic organisms. One classic example of such an enzyme is cobalamin-dependent methionine synthase (MS). MS is a large modular protein that utilizes an S2-type mechanism to catalyze the chemically challenging methyl transfer from the tertiary amine (N5) of methyltetrahydrofolate to homocysteine in order to form methionine. Despite over half a century of study, many questions remain about how folate-dependent methyltransferases, and MS in particular, function. Here, the structure of the folate-binding (Fol) domain of MS from Thermus thermophilus is reported in the presence and absence of methyltetrahydrofolate. It is found that the methyltetrahydrofolate-binding environment is similar to those of previously described methyltransferases, highlighting the conserved role of this domain in binding, and perhaps activating, the methyltetrahydrofolate substrate. These structural studies further reveal a new distinct and uncharacterized topology in the C-terminal region of MS Fol domains. Furthermore, it is found that in contrast to the canonical TIM-barrel βα fold found in all other folate-binding domains, MS Fol domains exhibit a unique βα fold. It is posited that these structural differences are important for MS function. PubMed: 29372898DOI: 10.1107/S2059798317018290 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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