Correction for “ Structural basis of photosensitivity in a bacterial light - oxygen - voltage / helix - turn - helix ( LOV - HTH ) DNA - binding protein
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BIOPHYSICS AND COMPUTATIONAL BIOLOGY Correction for “Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein,” by Abigail I. Nash, Reginald McNulty, Mary Elizabeth Shillito, Trevor E. Swartz, Roberto A. Bogomolni, Hartmut Luecke, and Kevin H. Gardner, which appeared in issue 23, June 7, 2011, of Proc Natl Acad Sci USA (108:9449–9454; first published May 23, 2011; 10.1073/pnas.1100262108). The authors note that Fig. 3 appeared incorrectly. As originally published, the color scale in Fig. 3C was inadvertently reversed (with red indicating minimal chemical shift changes and blue indicating maximal changes upon illumination). The corrected figure and its legend appear below.
منابع مشابه
Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.
Light-oxygen-voltage (LOV) domains are blue light-activated signaling modules integral to a wide range of photosensory proteins. Upon illumination, LOV domains form internal protein-flavin adducts that generate conformational changes which control effector function. Here we advance our understanding of LOV regulation with structural, biophysical, and biochemical studies of EL222, a light-regula...
متن کاملDetecting DNA-binding helix–turn–helix structural motifs using sequence and structure information
In this work, we analyse the potential for using structural knowledge to improve the detection of the DNA-binding helix-turn-helix (HTH) motif from sequence. Starting from a set of DNA-binding protein structures that include a functional HTH motif and have no apparent sequence similarity to each other, two different libraries of hidden Markov models (HMMs) were built. One library included seque...
متن کاملStructural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA.
The photosensor YtvA binds flavin mononucleotide and regulates the general stress reaction in Bacillus subtilis in response to blue light illumination. It belongs to the family of light-oxygen-voltage (LOV) proteins that were first described in plant phototropins and form a subgroup of the Per-Arnt-Sim (PAS) superfamily. Here, we report the three-dimensional structure of the LOV domain of YtvA ...
متن کاملIdentifying DNA-binding proteins using structural motifs and the electrostatic potential.
Robust methods to detect DNA-binding proteins from structures of unknown function are important for structural biology. This paper describes a method for identifying such proteins that (i) have a solvent accessible structural motif necessary for DNA-binding and (ii) a positive electrostatic potential in the region of the binding region. We focus on three structural motifs: helix-turn-helix (HTH...
متن کاملThe helix-turn-helix motif of bacterial insertion sequence IS911 transposase is required for DNA binding.
The transposase of IS911, a member of the IS3 family of bacterial insertion sequences, is composed of a catalytic domain located at its C-terminal end and a DNA binding domain located at its N-terminal end. Analysis of the transposases of over 60 members of the IS3 family revealed the presence of a helix-turn-helix (HTH) motif within the N-terminal region. Alignment of these potential secondary...
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تاریخ انتشار 2012