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Cover Illustration: The NMR solution structure of KP-TerB, a tellurite-resistance protein from Klebsiella pneumoniae, has been determined on the basis of 2593 restraints. The protein is an all-alpha protein mainly composed of seven α-helices and a short 3₁₀ helix (residues 63–66) after helix III (yellow), with helices II–V apparently forming a four-helix bundle. A number of long-range NOEs were observed for the residues in helices I–VI so that the orientations of these helices were well defined. By contrast, the orientation of helix VII (light coral) could not be accurately determined due to the lack of long-range NOEs. The structural similarity search using DALI could not find any structure with a significant Z-score. Therefore, the protein sequence and structures of KP-TerB are unique. To the best of our knowledge, KP-TerB is the first reported 3D solution structure among all tellurite-resistance proteins. (See, Chiang et al. pp. 785–789.)