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Structure in an extreme environment: NMR at high salt.

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.

SUBMITTER: Binbuga B

PROVIDER: S-EPMC2203353 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature

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Structure in an extreme environment: NMR at high salt.

Binbuga Bulent B Boroujerdi Arezue F B AF Young John K JK

Protein science : a publication of the Protein Society 20070801 8

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 t ...[more]

PMID: 17656587

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