Crystal structures of native cytochrome c₆ from Thermosynechococcus elongatus in two different space groups and implications for its oligomerization.

ABSTRACT: Native cytochrome c₆ was purified from an extract of strain BP-1 of the thermophilic cyanobacterium Thermosynechococcus elongatus. The protein was crystallized, and with only slight modifications of the buffer and vapour-diffusion conditions two different space groups were observed, namely H3 and C2. Both crystal structures were solved; they contained three and six molecules per asymmetric unit and were refined to 1.7 and 2.25 Å resolution, respectively. To date, the structure of native cytochrome c₆ from T. elongatus has only been reported as a monomer using NMR spectroscopy, i.e. without addressing putative oligomerization, and related structures have only previously been solved using X-ray crystallography after recombinant gene overexpression in Escherichia coli. T

SUBMITTER: Falke S 

PROVIDER: S-EPMC7470040 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature