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2ith
From Proteopedia
Revision as of 02:37, 29 September 2014 by OCA (Talk | contribs)
2ith is a 1 chain structure with sequence from Haloferax volcanii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure in an extreme environment: NMR at high salt.,Binbuga B, Boroujerdi AF, Young JK Protein Sci. 2007 Aug;16(8):1783-7. PMID:17656587[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Binbuga B, Boroujerdi AF, Young JK. Structure in an extreme environment: NMR at high salt. Protein Sci. 2007 Aug;16(8):1783-7. PMID:17656587 doi:16/8/1783
