Crystal structures of phosphotransferase system enzymes PtxB (IIB(Asc)) and PtxA (IIA(Asc)) from Streptococcus mutans

Journal of Molecular Biology
Jian LeiXiao-Dong Su

Abstract

Streptococcus mutans is the primary etiological agent of dental caries in man and other mammalian organisms. This bacterium metabolizes carbohydrates actively and thrives under anaerobic conditions by fermenting l-ascorbate (Asc) via the sga operon, which includes SgaT, PtxB, and PtxA. These three proteins are members of the Asc family of enzyme II (EII) complexes of the bacterial phosphotransferase system. Here, we report the crystal structure of PtxB, solved by single-wavelength anomalous dispersion phasing, and that of PtxA, solved by molecular replacement, from S. mutans. PtxB provides the first crystal structure of an EIIB from the Asc family, composed of a central beta sheet of parallel strands flanked by alpha helices on both sides. The structure of PtxB is similar to the structures of IIB(Mtl) (IIB subunit of mannitol PTS) and IIB(Cel) (IIB subunit of cellobiose) in Escherichia coli despite the low sequence identity. PtxA adopts a globular alpha/beta sandwich structure. The phosphorylation-site His68 is situated between beta2 and beta3, within a hydrophobic pocket. We found that the hydrogen bond on N(delta1) of the active-site histidine is a common means of ensuring that phosphate is on the correct N(varepsilon2) site ...Continue Reading

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Citations

Aug 18, 2009·Biochemical and Biophysical Research Communications·Stefan ReineltKlaus Scheffzek
Jan 30, 2014·Journal of Structural and Functional Genomics·Lanfen LiXiao-Dong Su
May 25, 2016·Molecules and Cells·Jimin ParkDong Hae Shin

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