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Structural and functional analysis of the solute-binding protein UspC from Mycobacterium tuberculosis that is specific for amino sugars

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Fullam, Elizabeth, Prokes, Ivan, Fütterer, Klaus and Besra, Gurdyal S. (2016) Structural and functional analysis of the solute-binding protein UspC from Mycobacterium tuberculosis that is specific for amino sugars. Open Biology (6). doi:10.1098/rsob.160105 ISSN 2046-2441.

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Official URL: http://dx.doi.org/10.1098/rsob.160105

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Abstract

Mycobacterium tuberculosis (Mtb), the aetiological agent of tuberculosis, has evolved to scavenge nutrients from the confined environment of host macrophages with mycobacterial ATP-binding cassette (ABC) transporters playing a key role in nutrient acquisition. Mtb-UspC (Rv2318) is the solute-binding protein of the essential transporter UspABC, one of four Mtb ABC transporters implicated by homology in sugar acquisition. Herein, we report the structural and functional characterization of Mtb-UspC. The 1.5 Å resolution structure of UspC reveals a two subdomain architecture that forms a highly acidic carbohydrate-substrate binding cleft. This has allowed a distinct preference of Mtb-UspC for amino sugars as determined by thermal shift analysis and solution saturation transfer difference-NMR. Taken together our data support the functional assignment of UspABC as an amino-sugar transporter. Given the limited availability of carbohydrates within the phagosomal environmental niche during Mtb intracellular infection, our studies suggest that UspABC enables Mtb to optimize the use of scarce nutrients during intracellular infection, linking essentiality of this protein to a potential role in recycling components of cell-wall peptidoglycan.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Mycobacterium tuberculosis, Amino sugars, X-ray crystallography, ATP-binding cassette transporters, peptidoglycan
Journal or Publication Title: Open Biology
Publisher: The Royal Society Publishing
ISSN: 2046-2441
Official Date: May 2016
Dates:
DateEvent
May 2016Published
22 June 2016Available
26 May 2016Accepted
12 April 2016Submitted
Number: 6
DOI: 10.1098/rsob.160105
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 22 June 2016
Date of first compliant Open Access: 23 June 2016
Funder: Royal Society (Great Britain). Wolfson Research Merit Award (RSWRMA), Medical Research Council (Great Britain) (MRC), Leverhulme Trust (LT), Wellcome Trust (London, England), Royal Society (Great Britain)
Grant number: MR/K012118/1 (MRC), 104193/Z/14/Z (Wellcome Trust & Royal Society)

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