Extended Data Figure 1 : Domain organization of biotin-dependent carboxylases.

From: Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase

Extended Data Figure 1

a, Reactions catalysed by biotin-dependent carboxylases. Biotin is linked to the side chain of a Lys residue in BCCP, and this flexible arm has a maximum length of 16 Å. The BCCP domain must also translocate to reach both active sites, separated by distances of 40–85 Å based on known holoenzyme structures (swinging domain model). b, Domain organizations of several representative biotin-dependent carboxylases. Homologous domains are given the same colours. The CT domain of PC has a completely different sequence and structure from those of ACC and PCC. The proteins are drawn to scale, and a scale bar is shown at the bottom. BT, BC–CT interaction domain; PT, PC tetramerization domain, also known as allosteric domain. c, Chemical structures of the substrates of ACC, PCC, LCC, MCC and GCC. The site of carboxylation is indicated with the red arrow.