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Figure 5
Active site of AoAA13-His91flip. (a) The protein is shown in cyan with the His brace as sticks. The active-site residue His91 is modelled in a native (H91B) and non-native (H91A) conformation with 20 and 80% occupancy, respectively. (b) The 2FoFc (blue, at 1.0σ) and FoFc (green, at 2.0σ) maps shown as calculated for the fully occupied flipped conformation of His91 (100% occupancy of H91A). The fully ordered active site of Zn-AoAA13 (grey) is shown for comparison. (c) The active site of AoAA13-His91flip (the Thr220–Gln222–Tyr224 and Gly89–meHis1 interactions are lost) compared with Zn-AoAA13. The β5–β6 loop moves away from the active site. His91 flips out of the active site (H91A), interacting with Phe166. The vacant position of H91A is partly occupied by Gln222 and Gly89, which lose interactions with the active-site residues meHis1 and Tyr224.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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