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Publication Abstract from PubMed

The crystal structure of Ton1535, a hypothetical protein from Thermococcus onnurineus NA1, was determined at 2.3 A resolution. With two antiparallel alpha-helices in a helix-turn-helix motif as a repeating unit, Ton1535 consists of right-handed coiled N- and C-terminal regions that are stacked together using helix bundles containing a left-handed helical turn. One left-handed helical turn in the right-handed coiled structure produces two unique structural properties. One is the presence of separated concave grooves rather than one continuous concave groove, and the other is the contribution of alpha-helices on the convex surfaces of the N-terminal region to the extended surface of the concave groove of the C-terminal region and vice versa. Proteins 2013. (c) 2013 Wiley Periodicals, Inc.

Structure of the hypothetical protein Ton1535 from Thermococcus onnurineus NA1 reveals unique structural properties by a left-handed helical turn in normal alpha-solenoid protein.,Jeong JH, Kim YS, Rojvirija C, Jin Cha H, Kim YG, Chul Ha S Proteins. 2013 Nov 22. doi: 10.1002/prot.24444. PMID:24265202^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.