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FEMS Microbiol Lett. 2003 Jul 15;224(1):113-8.

Purification and characterization of KpsT, the ATP-binding component of the ABC-capsule exporter of Escherichia coli K1.

Author information

1
Department of Microbiology and Immunology, University of Rochester Medical Center, 601 Elmwood Ave., Box 672, Rochester, NY 14642, USA.

Abstract

The K1 capsule, an alpha(2,8)-linked polymer of sialic acid, is an important virulence determinant of invasive Escherichia coli. The 17-kb kps gene cluster of E. coli K1 encodes the information necessary for capsule expression at the cell surface. Two proteins, KpsM and KpsT, play a role in the transport of capsular polysaccharide across the cytoplasmic membrane, utilizing the energy from ATP hydrolysis. They belong to the ATP-binding cassette superfamily of transport proteins. In this study, we purified KpsT in its native form and show that the purified protein is able to bind ATP, undergo an ATP-dependent conformational change and hydrolyze ATP. Protease accessibility studies demonstrate the in vivo interaction between KpsM and KpsT.

PMID:
12855177
DOI:
10.1016/S0378-1097(03)00428-2
[Indexed for MEDLINE]
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