Premium
Structure in an extreme environment: NMR at high salt
Author(s) -
Binbuga Bulent,
Boroujerdi Arezue F.B.,
Young John K.
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.072950407
Subject(s) - halophile , haloferax volcanii , dihydrofolate reductase , extreme environment , salt (chemistry) , haloarchaea , protein structure , chemistry , crystal structure , crystallography , enzyme , stereochemistry , biochemistry , biology , bacteria , genetics , organic chemistry
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 β3 and the type of β‐turn connection β7 and β8.