4ZTY
Neurospora crassa cobalamin-independent methionine synthase complexed with Cd2+
Summary for 4ZTY
| Entry DOI | 10.2210/pdb4zty/pdb |
| Related | 4ZTX |
| Descriptor | Cobalamin-Independent Methionine synthase, CADMIUM ION, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | homocysteine, methyltetrahydrofolate, tim barrel (alpha/beta barrel), methionine synthesis, methyltransferase, transferase |
| Biological source | Neurospora crassa |
| Total number of polymer chains | 1 |
| Total formula weight | 87535.40 |
| Authors | Wheatley, R.W.,Ng, K.K.,Kapoor, M. (deposition date: 2015-05-15, release date: 2015-12-09, Last modification date: 2024-03-06) |
| Primary citation | Wheatley, R.W.,Ng, K.K.,Kapoor, M. Fungal cobalamin-independent methionine synthase: Insights from the model organism, Neurospora crassa. Arch.Biochem.Biophys., 590:125-137, 2015 Cited by PubMed Abstract: Two families of methionine synthases, distinct in catalytic and structural features, have been encountered: MetH, the cobalamin-dependent enzyme and MetE, the cobalamin-independent form. The MetE family is of mechanistic interest due to the chemically challenging nature of the reaction and is a potential target for antifungal therapeutics since the human genome encodes only MetH. Here we report the identification, purification, and crystal structure of MetE from the filamentous fungus Neurospora crassa (ncMetE). ncMetE was highly thermostable and crystallized readily, making it ideal for study. Crystal structures of native ncMetE in complex with either Zn(2+)or Cd(2+) were solved at resolution limits of 2.10 Å and 1.88 Å, respectively. The monomeric protein contains two domains, each containing a (βα)8 barrel core, and a long α-helical segment spans the length of the protein, connecting the domains. Zn(2+) bound in the C-terminal domain exhibits tetrahedral coordination with the side chains of His 652, Cys 654, Glu 676 and Cys 737. A Cd(2+) replete structure revealed a supermetalated enzyme and demonstrated the inate flexibility of the metal binding site. An extensive analysis of sequence conservation within the MetE family identified 57 highly conserved residues and 60 additional residues that were conserved in all fungal sequences examined. PubMed: 26657067DOI: 10.1016/j.abb.2015.11.037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.88 Å) |
Structure validation
Download full validation report
