Structural and biochemical studies of bacillus subtilis mobb

Dajeong Kim, Sarah Choi, Hyunjin Kim, Jungwoo Choe

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1 Scopus citations


The biosynthesis of molybdenum cofactor for redox enzymes is carried out by multiple enzymes in bacteria including MobA and MobB. MobA is known to catalyze the attachment of GMP to molybdopterin to form molybdopterin guanine dinucleotide. MobB is a GTP binding protein that enhances the activity of MobA by forming the MobA:MobB complex. However, the mechanism of activity enhancement by MobB is not well understood. The structure of Bacillus subtilis MobB was determined to 2.4 Å resolution and it showed an elongated homodimer with an extended β-sheet. Bound sulfate ions were observed in the Walker A motifs, indicating a possible phosphate-binding site for GTP molecules. The binding assay showed that the affinity between B. subtilis MobA and MobB increased in the presence of GTP, suggesting a possible role of MobB as an enhancer of MobA activity.

Original languageEnglish
Article number1262
Issue number10
StatePublished - Oct 2021


  • Bacillus subtilis
  • Crystallography
  • MobB
  • Molybdenum cofactor
  • Walker A motif


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