Taxonomic distribution of proteins containing MoCF_biosynth domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing MoCF_biosynth domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

X-ray crystal structure of the trimeric N-terminal domain of gephyrin.

Sola M, Kneussel M, Heck IS, Betz H, Weissenhorn W
J Biol Chem. 2001; 276: 25294-301

Gephyrin is a ubiquitously expressed protein that, in the central nervoussystem, forms a submembraneous scaffold for anchoring inhibitoryneurotransmitter receptors in the postsynaptic membrane. The N- andC-terminal domains of gephyrin are homologous to the Escherichia colienzymes MogA and MoeA, respectively, both of which are involved inmolybdenum cofactor biosynthesis. This enzymatic pathway is highlyconserved from bacteria to mammals, as underlined by the ability ofgephyrin to rescue molybdenum cofactor deficiencies in differentorganisms. Here we report the x-ray crystal structure of the N-terminaldomain (amino acids 2-188) of rat gephyrin at 1.9-A resolution.Gephyrin-(2-188) forms trimers in solution, and a sequence motif thoughtto be involved in molybdopterin binding is highly conserved betweengephyrin and the E. coli protein. The atomic structure of gephyrin-(2-188)resembles MogA, albeit with two major differences. The path of theC-terminal ends of gephyrin-(2-188) indicates that the central andC-terminal domains, absent in this structure, should follow a similar3-fold arrangement as the N-terminal region. In addition, a centralbeta-hairpin loop found in MogA is lacking in gephyrin-(2-188). Despitethese differences, both structures show a high degree of surface chargeconservation, which is consistent with their common catalytic function.