6knt

Crystal structure of the metallo-beta-lactamase fold protein YhfI from Bacillus subtilis (space group P4332)

spinqualitylabelsall models 6knt, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6knt is a 4 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E0TYN8_BACSH Publication Abstract from PubMed Metallo-beta-lactamase (MBL) fold proteins play critical roles in diverse biological processes, such as DNA repair, RNA processing, detoxification, and metabolism. Although MBL fold proteins share a metal-bound alphabetabetaalpha structure, they are highly heterogeneous in metal type, metal coordination, and oligomerization and exhibit different catalytic functions. Bacillus subtilis contains the yhfI gene, which is predicted to encode an MBL fold protein. To reveal the structural and functional features of YhfI, we determined two crystal structures of YhfI and biochemically characterized the catalytic activity of YhfI. YhfI forms an alpha-helix-decorated beta-sandwich structure and assembles into a dimer using highly conserved residues. Each YhfI chain simultaneously interacts with two metal ions, which are coordinated by histidine and aspartate residues that are strictly conserved in YhfI orthologs. A comparative analysis of YhfI and its homologous structures suggests that YhfI would function as a phosphodiesterase. Indeed, YhfI drove the phosphodiesterase reaction and showed high catalytic activity at pH 8.0-9.5 in the presence of manganese. Moreover, we propose that the active site of YhfI is located at a metal-containing pocket generated between the two subunits of a YhfI dimer. Structural and biochemical analyses of the metallo-beta-lactamase fold protein YhfI from Bacillus subtilis.,Na HW, Namgung B, Song WS, Yoon SI Biochem Biophys Res Commun. 2019 Oct 29;519(1):35-40. doi:, 10.1016/j.bbrc.2019.08.106. Epub 2019 Aug 31. PMID:31481231 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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