PDBsum entry: 1ihc

Contractile protein

PDB id: 1ihc

Contents

Protein chain

169 a.a. *

Waters ×90

* Residue conservation analysis

PDB id:

1ihc

Name:

Contractile protein

Title:

X-ray structure of gephyrin n-terminal domain

Structure:

Gephyrin. Chain: a. Fragment: n-terminal domain. Synonym: putative glycine receptor-tubulin linker protein. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Trimer (from PDB file)

Resolution:

1.90Å R-factor: 0.203 R-free: 0.219

Authors:

M.Sola,M.Kneussel,I.S.Heck,H.Betz,W.Weissenhorn

Key ref:

M.Sola et al. (2001). X-ray crystal structure of the trimeric N-terminal domain of gephyrin. J Biol Chem, 276, 25294-25301. PubMed id: 11325967 DOI: 10.1074/jbc.M101923200

Date:

21-Apr-01 Release date: 16-May-01

Protein chain

Q03555  (GEPH_RAT) -  Gephyrin

Seq: 768 a.a.

Struc: 169 a.a.

Enzyme reactions

• Enzyme class 2: E.C.2.10.1.1 - Molybdopterin molybdotransferase.
• Reaction: Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP
• Cofactor: Zinc or magnesium
• Enzyme class 3: E.C.2.7.7.75 - Molybdopterin adenylyltransferase.
• Reaction: ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
• Cofactor: Manganese or magnesium

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: Mo-molybdopterin cofactor biosynthetic process (1 term)

reference

DOI no: 10.1074/jbc.M101923200

J Biol Chem 276:25294-25301 (2001)

PubMed id: 11325967

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

M.Sola, M.Kneussel, I.S.Heck, H.Betz, W.Weissenhorn.

ABSTRACT

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.

Selected figure(s)

Figure 2.
Fig. 2. Ribbon diagram of gephyrin-(2-188). a (top view), secondary structure elements are labeled for one monomer. The positions of proposed active sites (MPT) are indicated by black arrows. Cter, C terminus; Nter, N terminus. b (side view), shows the path of the C-terminal -helix 8 connecting to the intervening domain of gephyrin. Positions of possible sequence insertions in differentially spliced gephyrin variants are indicated by yellow arrows (1, cassette 1; 5, cassette 5). C (close-up view), the linker sequence in stereo. Hydrogen bonds are shown as dashed lines. Figs. 2 and 5b were generated using the program MOLMOL (46).

Figure 4.
Fig. 4. Electrostatic potential maps of gephyrin-(2-188) (a and c) and MogA (b and d). Regions where electrostatic potential < 30 k[B]T are shown in red and those > +30 k[B]T are shown in blue (k[B], Boltzmann constant; T, absolute temperature). The surface changes between the gephyrin-(2-188) and the E. coli MogA structures caused by the insertion of a loop in MogA and the different paths of the C-terminal ends are indicated by yellow arrows. The surfaces viewed from the top (a and b) and bottom (c and d). White arrows indicate slight differences in the trimer interface as seen from the top.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 25294-25301) copyright 2001.

Figures were selected by an automated process.