PDBsum entry: 1fc5

Biosynthetic protein

PDB id: 1fc5

Contents

Protein chains

404 a.a. *

Metals

_MG ×2

Waters ×500

* Residue conservation analysis

PDB id:

1fc5

Name:

Biosynthetic protein

Title:

Crystal structure of molybdopterin biosynthesis moea protein

Structure:

Molybdopterin biosynthesis moea protein. Chain: a, b. Engineered: yes

Source:

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

Biol. unit:

Dimer (from PQS)

Resolution:

2.20Å R-factor: 0.253 R-free: 0.297

Authors:

W.Huang,M.Cygler,Montreal-Kingston Bacterial Structural Genomics Initiative (Bsgi)

Key ref:

J.D.Schrag et al. (2001). The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway. J Mol Biol, 310, 419-431. PubMed id: 11428898 DOI: 10.1006/jmbi.2001.4771

Date:

17-Jul-00 Release date: 25-Jul-01

Protein chains

P12281  (MOEA_ECOLI) -  Molybdopterin molybdenumtransferase

Seq: 411 a.a.

Struc: 404 a.a.

Enzyme reactions

• Enzyme class: E.C.2.10.1.1 - Molybdopterin molybdotransferase.
• Reaction: Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP
• Cofactor: Zinc or magnesium

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

 Gene Ontology (GO) functional annotation 

• Biological process: molybdopterin cofactor biosynthetic process (2 terms)
• Biochemical function: protein binding (3 terms)

Key reference

DOI no: 10.1006/jmbi.2001.4771

J Mol Biol 310:419-431 (2001)

PubMed id: 11428898

The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.

J.D.Schrag, W.Huang, J.Sivaraman, C.Smith, J.Plamondon, R.Larocque, A.Matte, M.Cygler.

ABSTRACT

MoeA is involved in synthesis of the molybdopterin cofactor, although its function is not yet clearly defined. The three-dimensional structure of the Escherichia coli protein was solved at 2.2 A resolution. The locations of highly conserved residues among the prokaryotic and eukaryotic MoeA homologs identifies a cleft in the dimer interface as the likely functional site. Of the four domains of MoeA, domain 2 displays a novel fold and domains 1 and 4 each have only one known structural homolog. Domain 3, in contrast, is structurally similar to many other proteins. The protein that resembles domain 3 most closely is MogA, another protein required for molybdopterin cofactor synthesis. The overall similarity between MoeA and MogA, and the similarities in a constellation of residues that are strongly conserved in MoeA, suggests that these proteins bind similar ligands or substrates and may have similar functions.

Selected figure(s)

Figure 6.
Figure 6. Molecular surface representation of the putative functional-site cleft. In this view, domain 2 of chain A is located above the cleft, and domains 3 (left) and 4 (right) of chain B are below the cleft. The surface is colored according to electrostatic potential ranging from -20 kT (red) to 10 kT (blue). The magnesium ion is shown in yellow and the coordinating water mol- ecules are shown in cyan. This Figure was produced using GRASP. 61

Figure 9.
Figure 9. Ribbon diagrams of (a) domain 3 of Moea, (b) MogA, (c) ModE, residues 3-82 and 195-233 (d) MobA. The molecules were superimposed with program Swiss- PDB Viewer 62 based on C a atoms and are shown in the same orien- tation. The greatest similarity is in the N-terminal portions of the domains (at the right in the view presented). Ions and ligands observed in the crystal structures, all bound at the C-terminal ends of the b-strands, are also shown.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 310, 419-431) copyright 2001.

Figures were selected by an automated process.