|
Figure 1.
Figure 1
Active site in F. oxysporum trypsin. The top row shows the change in the interaction
between the substrate and the catalytic serine and histidine, as well as Asp189 in the
specificity pocket in the ROOM, PH4 and PH5 structures. The distances of interest around
the substrate carbonyl group and in the specificity pocket are shown by dotted lines with
their lengths given in angstroms. W1 and W2 are two water molecules located in the active
site: W1 acts as the nucleophile and W2 as an activator by forming a strong hydrogen bond
to the substrate carbonyl O atom. In the bottom row, the same arrangement of residues is
shown. The protein atoms and coordinate axes are represented and coloured following the
same scheme as in Fig. 3[107] [link]-[108][turqarr.gif] to indicate their directional
motion. The orientation is the same as in Fig. 3[109] [link]-[110][turqarr.gif] . The
figure was created with MOLSCRIPT/RASTER3D (Kraulis, 1991[111] [Kraulis, P. J. (1991). J.
Appl. Cryst. 24, 946-950.]-[112][bluearr.gif] ; Merritt & Murphy, 1994[113] [Merritt, E.
A. & Murphy, M. E. (1994). Acta Cryst. D50, 869-873.]-[114][bluearr.gif] ).
|
