1ihc
From Proteopedia
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X-ray Structure of Gephyrin N-terminal Domain
Overview
Gephyrin is a ubiquitously expressed protein that, in the central nervous, system, forms a submembraneous scaffold for anchoring inhibitory, neurotransmitter receptors in the postsynaptic membrane. The N- and, C-terminal domains of gephyrin are homologous to the Escherichia coli, enzymes MogA and MoeA, respectively, both of which are involved in, molybdenum cofactor biosynthesis. This enzymatic pathway is highly, conserved from bacteria to mammals, as underlined by the ability of, gephyrin to rescue molybdenum cofactor deficiencies in different, organisms. Here we report the x-ray crystal structure of the N-terminal, domain (amino acids 2-188) of rat gephyrin at 1.9-A resolution., Gephyrin-(2-188) forms trimers in solution, and a sequence motif thought, to be involved in molybdopterin binding is highly conserved between, gephyrin and the E. coli protein. The atomic structure of gephyrin-(2-188), resembles MogA, albeit with two major differences. The path of the, C-terminal ends of gephyrin-(2-188) indicates that the central and, C-terminal domains, absent in this structure, should follow a similar, 3-fold arrangement as the N-terminal region. In addition, a central, beta-hairpin loop found in MogA is lacking in gephyrin-(2-188). Despite, these differences, both structures show a high degree of surface charge, conservation, which is consistent with their common catalytic function.
About this Structure
1IHC is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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 Jul 6;276(27):25294-301. Epub 2001 Apr 26. PMID:11325967
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