The hyperthermophile chromosomal protein Sac7d sharply kinks DNA

By H. Robinson, Y. Gao, B. S. McCrary, S. Edmondson, J. Shriver, A. Wang. 1998

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Pushing the limits of what is achievable in protein–DNA docking: benchmarking HADDOCK’s performance (2010, neutral): “‘Intermediate’ 1azp (51) Act: W24 ) G3,G15 V26,M29,S31,V45 ) C2-A4, T13-G15 (K22,T33,R42) ) T5-G7,C10-A12 Act: C2,G3,A4,T5,C6,G7, C10,G11,A12,T13,C14,G15 (52–55)”
Partial B-to-A DNA transition upon minor groove binding of protein Sac7d monitored by Raman spectroscopy. (2004, background): “The structures of several Sac7d/ Sso7d-DNA complexes have been studied by X-ray crystallography (6-8), NMR (9), and low-angle X-ray scattering (10).”
Posttranslational Protein Modification in Archaea (2005, background): “Instead, crenarchaeal species contain small, basic DNA-binding proteins thought to fulfill the same functions as histones, based on their physical properties (63, 64, 149, 355, 367, 466).”
An overview of the structures of protein-DNA complexes (2000, unknown): “A2(103-160), B1(5-75), B2(102-161) 1oct C1(5-75) Oct-1 POU domain H.”
The Major Architects of Chromatin: Architectural Proteins in Bacteria, Archaea and Eukaryotes (2008, background): “The DNAinteracting surface is a triple-stranded β-sheet and the DNA is bent away from the protein (Robinson et al., 1998), which is opposite to the way DNA is bent by bacterial HU.”