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Protein Science (2007), 16:1783-1787. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

Structure in an extreme environment: NMR at high salt

Bulent Binbuga, Arezue F.B. Boroujerdi, and John K. Young

Department of Chemistry, Mississippi State University, Mississippi State, Mississippi 39762, USA

(RECEIVED April 18, 2007; FINAL REVISION May 21, 2007; ACCEPTED May 23, 2007)

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.

Keywords: Haloferax volcanii; dihydrofolate reductase; high salt; NMR; structure calculation


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