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Figure 3.
Figure 3. Stereo view of the superposition of the closed
structure of TmPGK (black) with the open structure of BsPGK
(red). The central water of the TmPGK structure is shown in
blue. A large motion of residue Thr374 (Thr371; BsPGK) towards
Arg36 causes a subsequent reorientation of the C-terminal
residues Gly375-Gly377 (not labelled). The closed conformation
is locked by an inter-domain salt bridge between Arg62 and
Asp200 (green). The difference between the inter-domain angles
in TmPGK and BsPGK, a[TM] and a[BS], respectively, is 21°.
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