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2ITH

NMR Structure of Haloferax volcanii DHFR

Summary for 2ITH
Entry DOI10.2210/pdb2ith/pdb
NMR InformationBMRB: 6645
DescriptorDihydrofolate reductase (1 entity in total)
Functional Keywordsoxidoreductase, dihydrofolate reductase, dhfr, halophilic archaea
Biological sourceHaloferax volcanii
Total number of polymer chains1
Total formula weight17983.79
Authors
Binbuga, B. (deposition date: 2006-10-19, release date: 2007-09-04, Last modification date: 2024-05-01)
Primary citationBinbuga, 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: 17656587
DOI: 10.1110/ps.072950407
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

238895

數據於2025-07-16公開中

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