6C07
Crystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvum
Summary for 6C07
| Entry DOI | 10.2210/pdb6c07/pdb |
| Descriptor | S-adenosylmethionine synthase, CHLORIDE ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | s-adenosylmethionine synthetase, enzyme metabolism, anti-infective target, anti-cancer target, transferase |
| Biological source | Cryptosporidium parvum (strain Iowa II) |
| Total number of polymer chains | 4 |
| Total formula weight | 179864.26 |
| Authors | Ohren, J.F.,Viola, R.E. (deposition date: 2017-12-28, release date: 2019-01-16, Last modification date: 2023-10-04) |
| Primary citation | Ohren, J.,Parungao, G.G.,Viola, R.E. Structure of a critical metabolic enzyme: S-adenosylmethionine synthetase from Cryptosporidium parvum. Acta Crystallogr F Struct Biol Commun, 75:290-298, 2019 Cited by PubMed Abstract: S-Adenosyl-L-methionine (AdoMet), the primary methyl donor in most biological methylation reactions, is produced from ATP and methionine in a multistep reaction catalyzed by AdoMet synthetase. The diversity of group-transfer reactions that involve AdoMet places this compound at a key crossroads in amino-acid, nucleic acid and lipid metabolism, and disruption of its synthesis has adverse consequences for all forms of life. The family of AdoMet synthetases is highly conserved, and structures of this enzyme have been determined from organisms ranging from bacteria to humans. Here, the structure of an AdoMet synthetase from the infectious parasite Cryptosporidium parvum has been determined as part of an effort to identify structural differences in this enzyme family that can guide the development of species-selective inhibitors. This enzyme form has a less extensive subunit interface than some previously determined structures, and contains some key structural differences from the human enzyme in an allosteric site, presenting an opportunity for the design of selective inhibitors against the AdoMet synthetase from this organism. PubMed: 30950830DOI: 10.1107/S2053230X19002772 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
