Complete amino acid sequence and comparative molecular modelling of HPr from Streptococcus mutans Ingbritt.
The heat-stable phosphocarrier protein (HPr) of Streptococcus mutans was extracted from whole cells using sodium lauroylsarcosinate/EDTA and purified to homogeneity by a single-step, ion-exchange chromatographic procedure. The complete amino acid sequence of the protein was determined from peptides generated by trypsin, alpha-chymotrypsin, endoproteinase Glu-C, and cyanogen bromide treatment. The HPr from S. mutans contains 86 or 87 amino acyl residues, depending on removal of the N-terminal Met and the protein shows high sequence homology with HPr from other Gram-positive bacteria. The predicted tertiary structure of the S. mutans HPr, from model building by homology, is an open-faced beta-sandwich consisting of two alpha-helices and a four-stranded antiparallel beta-sheet.
Dashper
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SG
Biochemistry and Molecular Biology Unit, School of Dental Science, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Victoria, Australia.
Kirszbaum
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Huq
N L
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Riley
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PF
Reynolds
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EC
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002852:Chromatography, Ion Exchange; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013295:Streptococcus mutans / Q000378:metabolism*; D014357:Trypsin
D001426:Bacterial Proteins; D007202:Indicators and Reagents; D010446:Peptide Fragments; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide