2ITH
NMR Structure of Haloferax volcanii DHFR
Summary for 2ITH
Entry DOI | 10.2210/pdb2ith/pdb |
NMR Information | BMRB: 6645 |
Descriptor | Dihydrofolate reductase (1 entity in total) |
Functional Keywords | oxidoreductase, dihydrofolate reductase, dhfr, halophilic archaea |
Biological source | Haloferax volcanii |
Total number of polymer chains | 1 |
Total formula weight | 17983.79 |
Authors | Binbuga, B. (deposition date: 2006-10-19, release date: 2007-09-04, Last modification date: 2024-05-01) |
Primary citation | Binbuga, B.,Boroujerdi, A.F.,Young, J.K. Structure in an extreme environment: NMR at high salt. Protein Sci., 16:1783-1787, 2007 Cited by PubMed Abstract: Proteins from halophiles have adapted to challenging environmental conditions and require salt for their structure and function. How halophilic proteins adapted to a hypersaline environment is still an intriguing question. It is important to mimic the physiological conditions of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and represents the first high salt structure calculated using NMR data. Structure calculations show that this protein has a solution structure which is similar to the previously determined crystal structure with a difference at the N terminus of beta3 and the type of beta-turn connection beta7 and beta8. PubMed: 17656587DOI: 10.1110/ps.072950407 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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