Hanemaaijer R, Masurel R, Visser A J, de Kok A, Veeger C
Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.
FEBS Lett. 1988 Oct 10;238(2):285-8. doi: 10.1016/0014-5793(88)80498-8.
The dihydrolipoyl transacetylase (E2) component of A. vinelandii PDC and its lipoyl domain shows similar dynamic properties as revealed with fluorescence anisotropy decay of lipoyl-bound IAANS. The lipoyl domain (32.6 kDa), containing three almost identical subdomains shows a mode of rotation characteristic for a protein of about 30 kDa. A similar rotation is found in E2, indicating an independent rotational mobility of the whole domain in the multimeric E2 core (1.6 MDa). No independent rotation of a single lipoyl subdomain (10 kDa) is observed. The E1 component, in contrast to the E3 component, shows interaction with the lipoyl domain.
