5K2Y

Crystal structure of M. tuberculosis UspC (monoclinic crystal form)

Summary for 5K2Y

• Entry DOI: 10.2210/pdb5k2y/pdb
• Related: 5K2X
• Descriptor: Probable periplasmic sugar-binding lipoprotein UspC (2 entities in total)
• Functional Keywords: mycobacterium tuberculosis, abc transporter, solute binding protein, transport protein
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 89459.08

Authors

Futterer, K.,Fullam, E.,Besra, G.S. (deposition date: 2016-05-19, release date: 2016-06-01, Last modification date: 2024-05-08)

Primary citation

Fullam, E.,Prokes, I.,Futterer, K.,Besra, G.S.
Structural and functional analysis of the solute-binding protein UspC from Mycobacterium tuberculosis that is specific for amino sugars.
Open Biology, 6:-, 2016

PubMed 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.

PubMed: 27335320
DOI: 10.1098/rsob.160105

Experimental method

X-RAY DIFFRACTION (2.41 Å)