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![[Figure 3]](rr5052fig3mag.jpg)
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Figure 3
Active-site geometry of the T57V site-directed mutant of ADC. The protein is isostructural to WT ADC (PDB entry 1aw8; Albert et al., 1998  ) except in the region of the active site. Electron density is shown as a 2Fo − Fc map contoured at 1σ within 1.6 Å. (a, b) Electron density for the backbone from His19 to Cys26 is well defined in both protomers of the asymmetric unit. Electron density is evident for the β-hydroxyl of Ser25 and there is no evidence for the presence of an ester in the structure. (c) Overlay of the backbone structure for the two protomers in the asymmetric unit of the T57V mutant with the two protomers from the unprocessed WT protein (green, T57V protomer A; yellow, T57V protomer B; blue, WT protomer A; cyan, WT protomer B). Both protomers adopt a similar conformation distinct from either of the observed conformations in the unprocessed WT structure (PDB entry 1ppy; Schmitzberger et al., 2003). (d) Displacement of the unprocessed chain from the position observed in the unprocessed WT structure can be attributed to binding of malonate to Arg54 in the active site of the mutant. A bound water molecule is illustrated as a red sphere. |
![[Figure 3]](rr5052fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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