 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](mn5075fig4mag.jpg)
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Figure 4
(a) Stereo figure of the interactions of human mitochondrial 3-ketoacyl-CoA thiolase chain C and the CoA molecule together with the 2Fo − Fc map constructed at 1σ. Arg224 interacts with the adenine moiety of the CoA molecule and Thr227 is hydrogen-bonded to the N6A atom of CoA. The carbonyl O atom of Ser251 is hydrogen-bonded to the N8P atom of the pantetheine part of the CoA molecule. The two conserved active-site water molecules and the four active-site residues Cys92, Asn320, His352 and Cys382 are shown. Cys92 is oxidized in the CoA-bound hT1 structure (PDB entry 4c2j ). (b) Stereo figure of the superposition of CoA-bound human mitochondrial 3-ketoacyl-CoA thiolase (PDB entry 4c2j ) chain C (blue) with acetoacetyl-CoA-bound Z. ramigera thiolase (PDB entry 1m1o ) chain B (grey). The dotted lines visualize the hydrogen-bond interactions in OAH1 and OAH2. (c) PDB entry 4c2j chain C (blue) is superposed with acetyl-CoA-bound Z. ramigera thiolase chain B (PDB entry 1dm3 , yellow). In 1dm3 the active-site cysteine Cys89 is acetylated. The two active-site waters of hT1 and bacterial thiolase are coloured red and orange, respectively. |
![[Figure 4]](mn5075fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
