OhrR: Difference between revisions
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α-helix, α5, has a notable kink at residue G119. The dimerization interface is largely formed by three-ten helices (1a, 1b) and α1, α5, and α6 from each subunit. The extensive dimerization domain buries 5391Ų. Alignment of this reduced state with OhrR from Bacillus subtilus (PDB ID 1Z9C) shows that | α-helix, α5, has a notable kink at residue G119. The dimerization interface is largely formed by three-ten helices (1a, 1b) and α1, α5, and α6 from each subunit. The extensive dimerization domain buries 5391Ų. Alignment of this reduced state with OhrR from Bacillus subtilus (PDB ID 1Z9C) shows that | ||
[[Image:2pexlabeledchains.png|left| | [[Image:2pexlabeledchains.png|left|300px]]<br /> | ||
[[Image:2pex_aligned_to_1z9c_from_b_sub.png|center|250px]]<br /> | [[Image:2pex_aligned_to_1z9c_from_b_sub.png|center|250px]]<br /> | ||
==Oxidation-induced Confirmational Changes in OhrR Xc== | ==Oxidation-induced Confirmational Changes in OhrR Xc== | ||
