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Figure 2.
Figure 2. Structural analysis of 2-keto-3-deoxygluconate
kinase. (A) Stereo diagram of a structural alignment of TM0067
(blue) and 2-keto-3-deoxygluconate kinase from T. thermophilus
(PDB: 1v1a, grey), with bound ADP and 2-keto-3-deoxygluconate
(KDG) shown as spheres. (B) Stereo view of the active site, with
ADP, KDG, and the interacting residues shown in sticks. Carbon
atoms are colored light blue (TM0067), grey (T. thermophilus
enzyme), or yellow (ADP and KDG). Nitrogen, oxygen, and
phosphorus atoms are colored blue, red, and orange,
respectively. TM0067 residues are labeled; corresponding
residues in T. thermophilus are in parentheses. (C) Ribbon
diagram of the TM0067 hexamer. TM0067 forms a trimer of dimers,
where the flap region is shared between the monomers of each
dimer. In each dimer, one of the monomers is colored, while the
other is in grey.
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