1TLZ

Tsx structure complexed with uridine

Summary for 1TLZ

• Entry DOI: 10.2210/pdb1tlz/pdb
• Related: 1tlw 1tly
• Descriptor: Nucleoside-specific channel-forming protein tsx, URIDINE (3 entities in total)
• Functional Keywords: nucleoside transporter, beta barrel, uridine, membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P0A927
• Total number of polymer chains: 2
• Total formula weight: 65026.64

Authors

Ye, J.,van den Berg, B. (deposition date: 2004-06-10, release date: 2004-08-24, Last modification date: 2024-02-14)

Primary citation

Ye, J.,Van Den Berg, B.
Crystal structure of the bacterial nucleoside transporter Tsx.
Embo J., 23:3187-3195, 2004

PubMed Abstract: Tsx is a nucleoside-specific outer membrane (OM) transporter of Gram-negative bacteria. We present crystal structures of Escherichia coli Tsx in the absence and presence of nucleosides. These structures provide a mechanism for nucleoside transport across the bacterial OM. Tsx forms a monomeric, 12-stranded beta-barrel with a long and narrow channel spanning the outer membrane. The channel, which is shaped like a keyhole, contains several distinct nucleoside-binding sites, two of which are well defined. The base moiety of the nucleoside is located in the narrow part of the keyhole, while the sugar occupies the wider opening. Pairs of aromatic residues and flanking ionizable residues are involved in nucleoside binding. Nucleoside transport presumably occurs by diffusion from one binding site to the next.

PubMed: 15272310
DOI: 10.1038/sj.emboj.7600330

Experimental method

X-RAY DIFFRACTION (3.1 Å)