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Figure 4
A close-up view of the structure around amino-acid residue Ser85 in TSH2B. (a) A close-up view around the canonical H2B Asn84 residue, which corresponds to the TSH2B Ser85 residue in the nucleosome (PDB entry 3afa ; Tachiwana et al., 2010BB14). The H2B and H4 molecules are coloured yellow and pale cyan, respectively, and the side chains around the H2B Asn84 and H4 Arg78 residues are shown. The water-mediated hydrogen bonds between the H2B Asn84 and H4 Arg78 residues are depicted by dotted lines. The 2mFoDFc maps of the regions around the H2B Asn84 and H4 Arg78 residues were calculated and contoured at the 1.5σ level. (b) A close-up view around the TSH2B Ser85 residue in the nucleosome. The TSH2B and H4 molecules are coloured blue and pale cyan, respectively, and the side chains around the TSH2B Ser85 and H4 Arg78 residues are shown. The 2mFoDFc maps of the region around the TSH2B Ser85 and H4 Arg78 residues were calculated, and contoured at the 1.5σ level. (c)–(j) Close-up views of the TSH2B structure around the Thr33 (c), Ile42 (d), Ser61 (e), Thr68 (f), Ser76 (g), Ser85 (h), Ser91 (i) and Ser125 (j) residues. The corresponding regions of the H2B structure were superimposed. The TSH2B molecule is coloured blue, and the TSH2B Thr33, Ile42, Ser61, Thr68, Ser76, Ser85, Ser91 and Ser125 residues are coloured magenta. The H2B molecule is coloured grey.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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