6vfm

Crystal structure of SpeG allosteric polyamine acetyltransferase from Bacillus thuringiensis

spinqualitylabelsall models 6vfm, resolution 2.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6vfm is a 2 chain structure with sequence from Bacillus thuringiensis serovar finitimus YBT-020. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.67Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A437SL45_BACTU Publication Abstract from PubMed Polyamines are important for regulating biofilms and the exopolysaccharide of the biofilm matrix of Bacillus subtilis. Understanding how enzymes can regulate polyamine concentrations is critical for learning more about how these processes occur in diverse bacteria. Here, we describe the structure and function of another member of the spermidine/spermine acetyltransferases (SSAT) found in Bacilli. The SpeG enzyme from B. thuringiensis (BtSpeG) binds polyamines in its allosteric site and adopts a dodecameric oligomeric state similar to other SpeG enzymes from Gram-negative bacteria. Our kinetic results show the catalytic efficiency of BtSpeG was greater than any previously characterized SpeG to date, and in contrast to other SpeG proteins it exhibited very similar kinetic properties toward both spermine and spermidine. Similar to the SpeG enzyme from E. coli, BtSpeG was able to acetylate spermidine on the N(1) and N(8) positions. The turnover of BtSpeG toward spermine and spermidine was also two to three orders of magnitude greater than any other Bacilli SSAT enzyme that has been previously characterized. SpeG proteins from Bacilli, including B. cereus, B. thuringiensis and B. anthracis share nearly identical sequences and therefore our results likely provide insight into the structure/function relationship across multiple Bacillus species. SpeG polyamine acetyltransferase enzyme from Bacillus thuringiensis forms a dodecameric structure and exhibits high catalytic efficiency.,Tsimbalyuk S, Shornikov A, Thi Bich Le V, Kuhn ML, Forwood JK J Struct Biol. 2020 Jun 1;210(3):107506. doi: 10.1016/j.jsb.2020.107506. Epub, 2020 Apr 10. PMID:32283314 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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