Jen Hsin, Chris Chipot, and Klaus Schulten.
A glycophorin A-like framework for the dimerization of
photosynthetic core complexes.
Journal of the American Chemical Society, 131:17096-17098,
2009.
(PMC: 2792896)
HSIN2009A
The core complex in photosynthetic bacteria plays a central role in photosynthesis. This
molecular assembly is composed of two protein
complexes, viz., the light-harvesting complex I (LH1), which absorbs sunlight by
means of the protein-bound bacteriochlorophylls, and the
reaction center (RC), which uses the light-excitation energy absorbed by the LH
complexes to produce a transmembrane (TM) charge gradient,
subsequently employed for energy conversion. In Rhodobacter (Rba.) sphaeroides,
the core complex contains, in addition, two copies of the
single TM -helix protein, PufX, and forms a (RC-LH1-PufX) dimer. To this
date, no high-resolution structure has been reported for the
entire core complex. In particular, the location of PufX within the (RC-LH1-PufX)
dimer is still the subject of much debate. Here, one of
the proposed locations for PufX, requiring its dimerization, is examined. The PufX-dimer
model on the basis of the glycophorin A (GpA)
dimer was constructed, and its robustness was probed through a series of molecular
dynamics (MD) simulations. The free-energy change due
to the replacement of Gly35 by valine was also determined to assess whether this
mutation is responsible for distinct PufX oligomerization
states in different Rba. species. The present study shows that PufX helices form a
stable GpA-like dimer with a helix-helix crossing angle
that could constitute the molecular basis of the reported highly bent and V-shaped
structure of the Rba. sphaeroides core complex dimer.
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