 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 6]](mn5075fig6mag.jpg)
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Figure 6
(a) Stereo figure of superposition of the tetrameric medium-chain-specific degradative human mitochondrial 3-ketoacyl-CoA thiolase (PDB entry 4c2j ) chain C (blue) with the dimeric long-chain-specific degradative yeast peroxisomal AB-thiolase (PDB entry 1afw ) chain A (yellow), highlighting the structural differences in the Lα1 and covering loop region. The 2-methyl-2,4-pentanediol (MPD) in the AB-thiolase structure and CoA in 4c2j are shown as sticks in green and cyan, respectively. The binding site for MPD is predicted to be the binding pocket for the fatty-acyl tail of the yeast peroxisomal degradative thiolase. (b) Stereo figure of superposition of the human mitochondrial 3-ketoacyl-CoA thiolase (PDB entry 4c2j ) with the Z. ramigera biosynthetic thiolase (PDB entry 1dm3 ), showing that the water trail present in the Z. ramigera thiolase cannot be present in the hT1 structure. The Z. ramigera thiolase is shown in yellow and the waters in orange; this water trail extends from the active site to the back side of the molecule. hT1 is coloured blue and the waters are shown in red. The 1dm3 water trail is blocked in hT1 by the side chains of Val319 and the two tyrosines Tyr327 and Tyr182. In the Z. ramigera biosynthetic thiolase these residues are Ala315, Ala323 and Phe178, respectively. |
![[Figure 6]](mn5075fig6.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
