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![[Figure 1]](dw5167fig1mag.jpg)
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Figure 1
Overall structure of the S64A mutant and AmpC EC2. (a) A ribbon diagram shown with secondary structures labelled. The α-helical domain is coloured orange, while the α/β domain is coloured cyan and yellow. Strands β5–β8, the so-called Ω-loop, helices α3 and α15, and the R2 loop in the α/β domain are shown in cyan. Citrate molecules are shown as sticks. The location of the S64A mutation is highlighted by a red sphere. A dotted red line represents the disordered region (residues 286–294) harbouring the two-amino-acid insertion. The black circle indicates the region of AmpC EC2 that corresponds to the disordered R2 loop region of AmpC BER. (b) The initial maximum-likelihood weighted Fo − Fc electron-density map contoured at 3σ after molecular replacement for the citrate molecules in the final model is coloured black. (c) Superposition of the Cα traces of AmpC EC2 (green) and the S64A mutant (magenta). The black circle indicates the R2 loop region harbouring the two-amino-acid insertion. |
![[Figure 1]](dw5167fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
