6V6Y
Crystal Structure of T. thermophilus methylenetetrahydrofolate dehydrogenase (MTHFD)
Summary for 6V6Y
| Entry DOI | 10.2210/pdb6v6y/pdb |
| Descriptor | Bifunctional protein FolD, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | amino-acid biosynthesis, histidine biosynthesis, hydrolase, methionine biosynthesis, multifunctional enzyme, nadp, one-carbon metabolism, oxidoreductase, purine biosynthesis |
| Biological source | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
| Total number of polymer chains | 1 |
| Total formula weight | 30984.54 |
| Authors | Maiello, F.,Coelho, C.,Gallo, G.,Sucharski, F.,Hardy, L.,Wurtele, M. (deposition date: 2019-12-06, release date: 2020-05-27, Last modification date: 2023-10-11) |
| Primary citation | Maiello, F.,Gallo, G.,Coelho, C.,Sucharski, F.,Hardy, L.,Wurtele, M. Crystal structure of Thermus thermophilus methylenetetrahydrofolate dehydrogenase and determinants of thermostability. Plos One, 15:e0232959-e0232959, 2020 Cited by PubMed Abstract: The elucidation of mechanisms behind the thermostability of proteins is extremely important both from the theoretical and applied perspective. Here we report the crystal structure of methylenetetrahydrofolate dehydrogenase (MTHFD) from Thermus thermophilus HB8, a thermophilic model organism. Molecular dynamics trajectory analysis of this protein at different temperatures (303 K, 333 K and 363 K) was compared with homologous proteins from the less temperature resistant organism Thermoplasma acidophilum and the mesophilic organism Acinetobacter baumannii using several data reduction techniques like principal component analysis (PCA), residue interaction network (RIN) analysis and rotamer analysis. These methods enabled the determination of important residues for the thermostability of this enzyme. The description of rotamer distributions by Gini coefficients and Kullback-Leibler (KL) divergence both revealed significant correlations with temperature. The emerging view seems to indicate that a static salt bridge/charged residue network plays a fundamental role in the temperature resistance of Thermus thermophilus MTHFD by enhancing both electrostatic interactions and entropic energy dispersion. Furthermore, this analysis uncovered a relationship between residue mutations and evolutionary pressure acting on thermophilic organisms and thus could be of use for the design of future thermostable enzymes. PubMed: 32401802DOI: 10.1371/journal.pone.0232959 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15201566872 Å) |
Structure validation
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