1EX2

CRYSTAL STRUCTURE OF BACILLUS SUBTILIS MAF PROTEIN

Summary for 1EX2

• Entry DOI: 10.2210/pdb1ex2/pdb
• Related PRD ID: PRD_900003
• Descriptor: PROTEIN MAF, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: b. subtilis protein maf, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 43273.98

Authors

Minasov, G.,Teplova, M.,Stewart, G.C.,Koonin, E.V.,Anderson, W.F.,Egli, M.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2000-04-28, release date: 2000-06-14, Last modification date: 2024-11-20)

Primary citation

Minasov, G.,Teplova, M.,Stewart, G.C.,Koonin, E.V.,Anderson, W.F.,Egli, M.
Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP.
Proc.Natl.Acad.Sci.USA, 97:6328-6333, 2000

PubMed Abstract: Three-dimensional structures of functionally uncharacterized proteins may furnish insight into their functions. The potential benefits of three-dimensional structural information regarding such proteins are particularly obvious when the corresponding genes are conserved during evolution, implying an important function, and no functional classification can be inferred from their sequences. The Bacillus subtilis Maf protein is representative of a family of proteins that has homologs in many of the completely sequenced genomes from archaea, prokaryotes, and eukaryotes, but whose function is unknown. As an aid in exploring function, we determined the crystal structure of this protein at a resolution of 1.85 A. The structure, in combination with multiple sequence alignment, reveals a putative active site. Phosphate ions present at this site and structural similarities between a portion of Maf and the anticodon-binding domains of several tRNA synthetases suggest that Maf may be a nucleic acid-binding protein. The crystal structure of a Maf-nucleoside triphosphate complex provides support for this hypothesis and hints at di- or oligonucleotides with either 5'- or 3'-terminal phosphate groups as ligands or substrates of Maf. A further clue comes from the observation that the structure of the Maf monomer bears similarity to that of the recently reported Methanococcus jannaschii Mj0226 protein. Just as for Maf, the structure of this predicted NTPase was determined as part of a structural genomics pilot project. The structural relation between Maf and Mj0226 was not apparent from sequence analysis approaches. These results emphasize the potential of structural genomics to reveal new unexpected connections between protein families previously considered unrelated.

PubMed: 10841541
DOI: 10.1073/pnas.97.12.6328

Experimental method

X-RAY DIFFRACTION (1.85 Å)