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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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WRAP_160105.full_.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (1519Kb) | Preview |
Official URL: http://dx.doi.org/10.1098/rsob.160105
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 | ||||||||||
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| 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: |
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| 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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