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Figure 1
Crystal structure of BVU2987 from B. vulgatus. (a) Stereo ribbon diagram of the BVU2987 monomer with the N-terminal domain in cyan and the C-terminal tandem-repeat domain in pink. Helices H1–H4 (helices H1 and H3 are 310-helices and helices H2 and H4 are α-helices) and β-strands β1–β8 are indicated. (b) Diagram showing the secondary-structural elements of BVU2987 superimposed on its primary sequence. The α-helices, 310-helices and β-strands are indicated. The crystallized protein (including residues 20–145) was expressed with a tag that was removed during purification, leaving Gly0 followed by the target sequence (starting from residue 20). (c) The electrostatic surface potential reveals a prominent negatively charged region on the concave side of BVU2987 arising from the presence of numerous aspartic acid and glutamic acid residues (Asp21, Asp22, Glu54, Asp56, Asp59, Asp63, Glu73, Glu82, Glu116, Asp118, Glu123, Glu131, Asp142 and Asp144). The color scale is in units of ±kT/e.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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