3P5N

Structure and mechanism of the S component of a bacterial ECF transporter

Summary for 3P5N

• Entry DOI: 10.2210/pdb3p5n/pdb
• Descriptor: Riboflavin uptake protein, RIBOFLAVIN (2 entities in total)
• Functional Keywords: transporter, alpha-helical bundle, transport protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 42803.73

Authors

Zhang, P.,Wang, J.,Shi, Y. (deposition date: 2010-10-09, release date: 2010-11-03, Last modification date: 2024-03-20)

Primary citation

Zhang, P.,Wang, J.,Shi, Y.
Structure and mechanism of the S component of a bacterial ECF transporter
Nature, 468:717-720, 2010

PubMed Abstract: The energy-coupling factor (ECF) transporters, responsible for vitamin uptake in prokaryotes, are a unique family of membrane transporters. Each ECF transporter contains a membrane-embedded, substrate-binding protein (known as the S component), an energy-coupling module that comprises two ATP-binding proteins (known as the A and A' components) and a transmembrane protein (known as the T component). The structure and transport mechanism of the ECF family remain unknown. Here we report the crystal structure of RibU, the S component of the ECF-type riboflavin transporter from Staphylococcus aureus at 3.6-Å resolution. RibU contains six transmembrane segments, adopts a previously unreported transporter fold and contains a riboflavin molecule bound to the L1 loop and the periplasmic portion of transmembrane segments 4-6. Structural analysis reveals the essential ligand-binding residues, identifies the putative transport path and, with sequence alignment, uncovers conserved structural features and suggests potential mechanisms of action among the ECF transporters.

PubMed: 20972419
DOI: 10.1038/nature09488

Experimental method

X-RAY DIFFRACTION (3.6 Å)