3QE7

Crystal Structure of Uracil Transporter--UraA

Summary for 3QE7

• Entry DOI: 10.2210/pdb3qe7/pdb
• Descriptor: Uracil permease, URACIL, nonyl beta-D-glucopyranoside (3 entities in total)
• Functional Keywords: uracil permease, uracil transporter, uraa, transporter, inner membrane protein, transport protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0AGM7
• Total number of polymer chains: 1
• Total formula weight: 45508.29

Authors

Lu, F.R.,Li, S.,Yan, N. (deposition date: 2011-01-20, release date: 2011-03-23, Last modification date: 2024-03-20)

Primary citation

Lu, F.,Li, S.,Jiang, Y.,Jiang, J.,Fan, H.,Lu, G.,Deng, D.,Dang, S.,Zhang, X.,Wang, J.,Yan, N.
Structure and mechanism of the uracil transporter UraA
Nature, 472:243-246, 2011

PubMed Abstract: The nucleobase/ascorbate transporter (NAT) proteins, also known as nucleobase/cation symporter 2 (NCS2) proteins, are responsible for the uptake of nucleobases in all kingdoms of life and for the transport of vitamin C in mammals. Despite functional characterization of the NAT family members in bacteria, fungi and mammals, detailed structural information remains unavailable. Here we report the crystal structure of a representative NAT protein, the Escherichia coli uracil/H(+) symporter UraA, in complex with uracil at a resolution of 2.8 Å. UraA has a novel structural fold, with 14 transmembrane segments (TMs) divided into two inverted repeats. A pair of antiparallel β-strands is located between TM3 and TM10 and has an important role in structural organization and substrate recognition. The structure is spatially arranged into a core domain and a gate domain. Uracil, located at the interface between the two domains, is coordinated mainly by residues from the core domain. Structural analysis suggests that alternating access of the substrate may be achieved through conformational changes of the gate domain.

PubMed: 21423164
DOI: 10.1038/nature09885

Experimental method

X-RAY DIFFRACTION (2.781 Å)