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Figure 2
Amino-acid sequence alignment of various tetrameric thiolases. The secondary structure of human mitochondrial 3-ketoacyl-CoA thiolase (hT1) is indicated above the sequence. The N-domain secondary structure is in green, the loop domain (residues Tyr127–Val253) is in yellow and the C-domain is in red. The four catalytic loops are indicated with dashed lines below the sequence and the two active-site cysteines are marked with stars. The two regions in the active site that are different between hT1 and Z. ramigera thiolase are highlighted by # (Nβ2–Nα2) and * (Lα1). The amino-acid sequences of T1 (T1_HUM), T2 (T2_HUM) and CT (CT_HUM) from human, T1 from Sus scrofa (T1_PIG), Mus musculus (T1_MUS) and Rattus norvegicus (T1_RAT), and CT from Z. ramigera (CT_ZRA) were aligned using ClustalW (Larkin et al., 2007BB30) and the figure was prepared with ESPript (Gouet et al., 1999BB20).

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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