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Fig. 1. Structure of EGFP-gephyrin deletion constructs and mutant constructs. (A) Scheme of the five truncated gephyrin constructs and the construct with E-domain duplication. All constructs were coupled to EGFP at the N-terminus. First and last residues of the G and E domains as well as terminating residues are highlighted; L1 and L2 indicate the position of the two loops investigated in the mutant constructs (587-592 and 611-622, respectively). (B) Sequence of Loop 1 (L1) and Loop 2 (L2) mutant constructs, created by swapping residues from rat gephyrin (green boxes) with the corresponding E. coli MoeA residues (red boxes). L2A, L2B and L2C are three variants differing in the number of swapped residues: L2A (T611-F622), L2B (D613-I620), L2C (I614-K619). Boundary sequences in MoeA and gephyrin are indicated. Gray shading depicts the degree of conservation across species: black, 100% conservation; gray with black letters, at least 70% conservation; gray with white letters, type of amino acid conserved; white with black letters, variable. (C) Structure of gephyrin-E dimer shown in trace mode. The subdomains of one monomer are shown in shades of red and orange whereas the other monomer is shown in gray. Loops 1 and 2 are highlighted in light blue. For comparison, the active site of Moco synthesis is highlighted. (D) Zoom of subdomain 3 of panel C with the first and last residues that were exchanged in the corresponding L1 and L2 variants. Figures were generated with MOLSCRIPT (Esnouf, 1997) and rendered with POVRAY (www.povray.org).

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