Figure 6 | Scientific Reports

Figure 6

From: Structure of polyhydroxyalkanoate (PHA) synthase PhaC from Chromobacterium sp. USM2, producing biodegradable plastics

Figure 6

Conformational changes in the CAP subdomain induce dimer organization as revealed by comparison of PhaC Cs -CAT and PhaC Cn -CAT dimers. (a) Overlay of the PhaC Cs -CAT dimer (cyan and green) on the PhaC Cn -CAT dimer (gray and purple). One protomer (cyan) of the PhaC Cs -CAT dimer is superimposed on one protomer (gray) of the PhaC Cn -CAT dimer. The distance between the catalytic cysteine residues in the PhaC Cs -CAT dimer is 28.1 Å, while that in the PhaC Cn -CAT dimer is 33.3 Å. (b) The PhaC Cs -CAT dimer. The distance between the N-termini is 19.2 Å. (c) The PhaC Cn -CAT dimer with mol A in the same orientation as mol A in the PhaC Cs -CAT dimer as in (b). The dimer interface is reorganized by refolding/unfolding of the LID region with accompanying rotation of one protomer. The distance between the N-termini is 55.1 Å.

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