1FC5

CRYSTAL STRUCTURE OF MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN

Summary for 1FC5

• Entry DOI: 10.2210/pdb1fc5/pdb
• Descriptor: MOLYBDOPTERIN BIOSYNTHESIS MOEA PROTEIN, MAGNESIUM ION (3 entities in total)
• Functional Keywords: molybdopterin, four modules, with magnesium, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, biosynthetic protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 89011.04

Authors

Huang, W.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2000-07-17, release date: 2001-07-25, Last modification date: 2024-10-16)

Primary citation

Schrag, J.D.,Huang, W.,Sivaraman, J.,Smith, C.,Plamondon, J.,Larocque, R.,Matte, A.,Cygler, M.
The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.
J.Mol.Biol., 310:419-431, 2001

PubMed 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.

PubMed: 11428898
DOI: 10.1006/jmbi.2001.4771

Experimental method

X-RAY DIFFRACTION (2.2 Å)