Document Detail

Purification and characterization of KpsT, the ATP-binding component of the ABC-capsule exporter of Escherichia coli K1.
MedLine Citation:
PMID:  12855177     Owner:  NLM     Status:  MEDLINE    
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.
Christiane J Nsahlai; Richard P Silver
Related Documents :
9799497 - Fourier transform infrared analysis of purified lactose permease: a monodisperse lactos...
1748657 - Molecular characterization of the iron transport system mediated by the pjm1 plasmid in...
3223947 - The complete amino acid sequence of the human erythrocyte membrane anion-transport prot...
9528667 - Molecular cloning and functional expression of a rabbit renal organic cation transporter.
11206077 - The structure of the yrdc gene product from escherichia coli reveals a new fold and sug...
15293787 - Chitinase induced by jasmonic acid, methyl jasmonate, ethylene and protein phosphatase ...
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  FEMS microbiology letters     Volume:  224     ISSN:  0378-1097     ISO Abbreviation:  FEMS Microbiol. Lett.     Publication Date:  2003 Jul 
Date Detail:
Created Date:  2003-07-11     Completed Date:  2003-09-22     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  113-8     Citation Subset:  IM    
Department of Microbiology and Immunology, University of Rochester Medical Center, 601 Elmwood Ave., Box 672, Rochester, NY 14642, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
ATP-Binding Cassette Transporters / chemistry,  genetics,  isolation & purification,  metabolism*
Adenosine Triphosphatases / metabolism
Adenosine Triphosphate / analogs & derivatives*,  metabolism,  pharmacokinetics
Azides / pharmacokinetics
Bacterial Capsules / metabolism*
Escherichia coli / genetics,  metabolism*
Escherichia coli Proteins / chemistry,  genetics,  isolation & purification,  metabolism*
Membrane Transport Proteins / metabolism
Phosphorus Radioisotopes / diagnostic use
Protein Structure, Tertiary
Grant Support
Reg. No./Substance:
0/ATP-Binding Cassette Transporters; 0/Azides; 0/Bacterial Capsules; 0/Escherichia coli Proteins; 0/Membrane Transport Proteins; 0/Phosphorus Radioisotopes; 133135-12-3/kpsM protein, E coli; 133135-13-4/kpsT protein, E coli; 53696-59-6/8-azidoadenosine 5'-triphosphate; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Adenosine Triphosphatases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Identification and characterisation of the catalytic triad of the alkaliphilic thermotolerant PHA de...
Next Document:  The glutamate-dependent acid resistance system of Escherichia coli and Shigella flexneri is inhibite...