Acta Crystallographica Section D

Biological Crystallography

Volume 69, Part 10 (October 2013)

research papers

Acta Cryst. (2013). D69, 2050-2060    [ doi:10.1107/S0907444913018714 ]

Structural characterization of gephyrin by AFM and SAXS reveals a mixture of compact and extended states

B. Sander, G. Tria, A. V. Shkumatov, E.-Y. Kim, J. G. Grossmann, I. Tessmer, D. I. Svergun and H. Schindelin

Abstract: Gephyrin is a trimeric protein involved in the final steps of molybdenum-cofactor (Moco) biosynthesis and in the clustering of inhibitory glycine and GABAA receptors at post­synaptic specializations. Each protomer consists of stably folded domains (referred to as the G and E domains) located at either terminus and connected by a proteolytically sensitive linker of ~150 residues. Both terminal domains can oligomerize in their isolated forms; however, in the context of the full-length protein only the G-domain trimer is permanently present, whereas E-domain dimerization is prevented. Atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS) reveal a high degree of flexibility in the structure of gephyrin. The results imply an equilibrium between compact and extended conformational states in solution, with a preference for compact states. CD spectroscopy suggests that a partial compaction is achieved by interactions of the linker with the G and E domains. Taken together, the data provide a rationale for the role of the linker in the overall structure and the conformational dynamics of gephyrin.

Keywords: atomic force microscopy; ensemble-optimization method; gephyrin; glycine receptor; GABAA receptor; intrinsic disorder; Moco biosynthesis; receptor clustering; single-molecule analysis; small-angle X-ray scattering.

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