  Experiments have revealed that membrane proteins can form two-dimensional
clusters with regular translational and orientational protein arrangements,
which may allow cells to modulate protein function. However, the physical
mechanisms yielding supramolecular organization and collective function of
membrane proteins remain largely unknown. Here we show that bilayer-mediated
elastic interactions between membrane proteins can yield regular and
distinctive lattice architectures of protein clusters, and may provide a link
between lattice architecture and lattice function. Using the mechanosensitive
channel of large conductance (MscL) as a model system, we obtain relations
between the shape of MscL and the supramolecular architecture of MscL lattices.
We predict that the tetrameric and pentameric MscL symmetries observed in
previous structural studies yield distinct lattice architectures of MscL
clusters and that, in turn, these distinct MscL lattice architectures yield
distinct lattice activation barriers. Our results suggest general physical
mechanisms linking protein symmetry, the lattice architecture of membrane
protein clusters, and the collective function of membrane protein lattices.
