1FRW

STRUCTURE OF E. COLI MOBA WITH BOUND GTP AND MANGANESE

Summary for 1FRW

• Entry DOI: 10.2210/pdb1frw/pdb
• Descriptor: MOLYBDOPTERIN-GUANINE DINUCLEOTIDE BIOSYNTHESIS PROTEIN, ACETATE ION, ZINC ION, ... (6 entities in total)
• Functional Keywords: molybdenum cofactor (moco), moco biosynthesis, molybdopterin (mpt), molybdopterin guanine dinucleotide (mgd), metal binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 22372.42

Authors

Lake, M.W.,Temple, C.A.,Rajagopalan, K.V.,Schindelin, H. (deposition date: 2000-09-07, release date: 2001-01-10, Last modification date: 2024-02-07)

Primary citation

Lake, M.W.,Temple, C.A.,Rajagopalan, K.V.,Schindelin, H.
The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis.
J.Biol.Chem., 275:40211-40217, 2000

PubMed Abstract: The molybdenum cofactor (Moco) is found in a variety of enzymes present in all phyla and comprises a family of related molecules containing molybdopterin (MPT), a tricyclic pyranopterin with a cis-dithiolene group, as the invariant essential moiety. MPT biosynthesis involves a conserved pathway, but some organisms perform additional reactions that modify MPT. In eubacteria, the cofactor is often present in a dinucleotide form combining MPT and a purine or pyrimidine nucleotide via a pyrophosphate linkage. In Escherichia coli, the MobA protein links a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl(2), and the MPT form of the cofactor and can efficiently reconstitute Rhodobacter sphaeroides apo-DMSOR, an enzyme that requires molybdopterin guanine dinucleotide for activity. In this paper, we present the crystal structure of MobA, a protein containing 194 amino acids. The MobA monomer has an alpha/beta architecture in which the N-terminal half of the molecule adopts a Rossman fold. The structure of MobA has striking similarity to Bacillus subtilis SpsA, a nucleotide-diphospho-sugar transferase involved in sporulation. The cocrystal structure of MobA and GTP reveals that the GTP-binding site is located in the N-terminal half of the molecule. Conserved residues located primarily in three signature sequence motifs form crucial interactions with the bound nucleotide. The binding site for MPT is located adjacent to the GTP-binding site in the C-terminal half of the molecule, which contains another set of conserved residues presumably involved in MPT binding.

PubMed: 10978347
DOI: 10.1074/jbc.M007406200

Experimental method

X-RAY DIFFRACTION (1.75 Å)