PDBsum entry: 1r2k

Biosynthetic protein

PDB id: 1r2k

Contents

Protein chains

168 a.a. *

Ligands

SO4 ×2

Waters ×141

* Residue conservation analysis

PDB id:

1r2k

Name:

Biosynthetic protein

Title:

Crystal structure of moab from escherichia coli

Structure:

Molybdenum cofactor biosynthesis protein b. Chain: b, a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: moab, chla2, b0782, z1001, ecs0860. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Hexamer (from PQS)

Resolution:

2.10Å R-factor: 0.208 R-free: 0.250

Authors:

G.Bader,M.Gomez-Ortiz,C.Haussmann,A.Bacher,R.Huber,M.Fischer

Key ref:

G.Bader et al. (2004). Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli. Acta Crystallogr D Biol Crystallogr, 60, 1068-1075. PubMed id: 15159566 DOI: 10.1107/S0907444904007164

Date:

28-Sep-03 Release date: 01-Jun-04

Protein chains

P0AEZ9  (MOAB_ECOLI) -  Molybdenum cofactor biosynthesis protein B

Seq: 170 a.a.

Struc: 168 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: Mo-molybdopterin cofactor biosynthetic process (1 term)
• Biochemical function: nucleotide binding (2 terms)

DOI no: 10.1107/S0907444904007164

Acta Crystallogr D Biol Crystallogr 60:1068-1075 (2004)

PubMed id: 15159566

Structure of the molybdenum-cofactor biosynthesis protein MoaB of Escherichia coli.

G.Bader, M.Gomez-Ortiz, C.Haussmann, A.Bacher, R.Huber, M.Fischer.

ABSTRACT

The moaABC operon of Escherichia coli is involved in early steps of the biosynthesis of the molybdenum-binding cofactor molybdopterin, but the precise functions of the cognate proteins are not known. The crystal structure of the MoaB protein from E. coli was determined by multiple anomalous dispersion at 2.1 angstroms A resolution and refined to an R factor of 20.4% (Rfree = 25.0%). The protein is a 32-symmetric hexamer, with the monomers consisting of a central beta-sheet flanked by helices on both sides. The overall fold of the monomer is similar to those of the MogA protein of E. coli, the G-domains of rat and human gephyrin and the G-domains of Cnx1 protein from A. thaliana, all of which are involved in the insertion of an unknown molybdenum species into molybdopterin to form the molybdenum cofactor. Furthermore, the MoaB protein shows significant sequence similarity to the cinnamon protein from Drosophila melanogaster. In addition to other functions, all these proteins are involved in the biosynthesis of the molybdenum cofactor and have been shown to bind molybdopterin. The close structural homology to MogA and the gephyrin and Cnx1 domains suggests that MoaB may bind a hitherto unidentified pterin compound, possibly an intermediate in molybdopterin biosynthesis.

Selected figure(s)

Figure 1.
Figure 1 Ribbon representation of a MoaB monomer.

Figure 4.
Figure 4 Overlay of all MoaB homologues: MoaB (blue), MogA (red), Cnx1 G-domain (green), rat gephyrin (brown) and human gephyrin (grey). The sulfate ions conserved in MoaB and MogA are depicted in yellow and red, respectively.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1068-1075) copyright 2004.

Figures were selected by an automated process.