COMPLETE AMINO-ACID-SEQUENCE AND COMPARATIVE MOLECULAR MODELING OF HPR FROM STREPTOCOCCUS-MUTANS INGBRITT

被引：4

作者：

DASHPER, SG ^{[1
]}

KIRSZBAUM, L ^{[1
]}

HUQ, NL ^{[1
]}

RILEY, PF ^{[1
]}

REYNOLDS, EC ^{[1
]}

机构：

[1] UNIV MELBOURNE,FAC MED DENT & HLTH SCI,SCH DENT SCI,BIOCHEM & MOLEC BIOL UNIT,711 ELIZABETH ST,MELBOURNE,VIC 3000,AUSTRALIA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 199卷 / 03期

关键词：

D O I：

10.1006/bbrc.1994.1372

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1994 Academic Press, Inc.

引用

页码：1297 / 1304

页数：8

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