PDBsum entry: 1di6

Unknown function

PDB id: 1di6

Contents

Protein chain

183 a.a. *

Ligands

SO4 ×3

Waters ×128

* Residue conservation analysis

PDB id:

1di6

Name:

Unknown function

Title:

1.45 a crystal structure of the molybdenumm cofactor biosynt protein moga from escherichia coli

Structure:

Molybdenum cofactor biosynthetic enzyme. Chain: a. Synonym: moga. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Trimer (from PDB file)

Resolution:

1.45Å R-factor: 0.187 R-free: 0.213

Authors:

M.T.W.Liu,M.M.Wuebbens,K.V.Rajagopalan,H.Schindelin

Key ref:

M.T.Liu et al. (2000). Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli. J Biol Chem, 275, 1814-1822. PubMed id: 10636880 DOI: 10.1074/jbc.275.3.1814

Date:

29-Nov-99 Release date: 19-Jan-00

Protein chain

P0AF03  (MOG_ECOLI) -  Molybdopterin adenylyltransferase

Seq: 195 a.a.

Struc: 183 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.7.7.75 - Molybdopterin adenylyltransferase.
• Reaction: ATP + molybdopterin = diphosphate + adenylyl-molybdopterin
• Cofactor: Manganese or magnesium

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)
• Biochemical function: nucleotide binding (3 terms)

reference

DOI no: 10.1074/jbc.275.3.1814

J Biol Chem 275:1814-1822 (2000)

PubMed id: 10636880

Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli.

M.T.Liu, M.M.Wuebbens, K.V.Rajagopalan, H.Schindelin.

ABSTRACT

Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway in archaea, eubacteria, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in this biosynthetic pathway trigger an autosomal recessive disease with severe neurological symptoms, which usually leads to death in early childhood. The MogA protein exhibits affinity for molybdopterin, the organic component of Moco, and has been proposed to act as a molybdochelatase incorporating molybdenum into Moco. MogA is related to the protein gephyrin, which, in addition to its role in Moco biosynthesis, is also responsible for anchoring glycinergic receptors to the cytoskeleton at inhibitory synapses. The high resolution crystal structure of the Escherichia coli MogA protein has been determined, and it reveals a trimeric arrangement in which each monomer contains a central, mostly parallel beta-sheet surrounded by alpha-helices on either side. Based on structural and biochemical data, a putative active site was identified, including two residues that are essential for the catalytic mechanism.

Selected figure(s)

Figure 2.
Fig. 2. Ribbon representations of the MogA structure. A, the MogA monomer viewed perpendicular to the central -sheet. -Strands are shown as curved arrows in green, and -helices and the 3[10] helix are shown as ribbons in red and blue, respectively. Secondary structure elements, N and C termini, and the residues adjacent to the disordered loop are labeled. The sulfate molecule bound near the TXGGTG motif is indicated. B, the MogA monomer viewed along the -sheet and superimposed with a transparent surface representation of the protein. Note the pocket in the molecular surface located between 5 and the 3[10] helix. C, structure of the MogA trimer viewed along the 3-fold axis. Each color represents a different monomer. In addition to the sulfate, the side chains of the strictly conserved residues Asp-49 and Asp-82 are shown. Figs. 2, 3B, and 5B were produced with Molscript (42) and Raster3D (43).

Figure 3.
Fig. 3. Structural features of MogA. A, stereo view of the electron density maps (SIGMAA weighted 2F[o] F[c] and F[o] F[c] maps in blue and red, respectively) near the TXGGTG motif. Note the density feature extending from one of the sulfate oxygens (marked by the arrow). An additional unassigned peak is present at the bottom of the figure. Figs. 3A and 5A were prepared with SPOCK (44). B, least squares superposition of the NatH1 (dark gray) and NatH2 (light gray) structures. Residues 107-113 are shown with their side chains and adjacent regions of the molecule as C -trace.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2000, 275, 1814-1822) copyright 2000.

Figures were selected by an automated process.