PRELIMINARY CRYSTALLOGRAPHIC DATA OF RECEPTORS FOR TRANSPORT AND CHEMOTAXIS IN ESCHERICHIA-COLI - D-GALACTOSE AND MALTOSE-BINDING PROTEINS

被引:31
作者
QUIOCHO, FA
MEADOR, WE
PFLUGRATH, JW
机构
[1] Department of Biochemistry Rice University Houston
基金
美国国家卫生研究院;
关键词
D O I
10.1016/0022-2836(79)90256-0
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
We have obtained single crystals of maltose-binding protein (Mr = 40,500) and d-galactose-binding protein (Mr = 32,000), chemoreceptors for active transport and chemotaxis in Escherichia coli. This brings to a total of five the binding proteins that we have thus far crystallized; they include the l-arabinose-binding protein, the leucine, isoleucine, valine-binding protein from Escherichia coli, and a sulfate-binding protein from Salmonella typhimurium. The crystal structure of the l-arabinose-binding protein has been determined at 2.8 Å resolution (Quiocho et al., 1977a). © 1979.
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页码:181 / 184
页数:4
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