5EDL

Crystal structure of an S-component of ECF transporter

Summary for 5EDL

• Entry DOI: 10.2210/pdb5edl/pdb
• Descriptor: Putative HMP/thiamine permease protein YkoE, 3-(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-5-(2-HYDROXY-ETHYL)-4-METHYL-THIAZOL-3-IUM, [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate, ... (4 entities in total)
• Functional Keywords: membrane transport protein, transport protein
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane ; Multi-pass membrane protein : O34738
• Total number of polymer chains: 1
• Total formula weight: 21959.60

Authors

Josts, I.,Tidow, H. (deposition date: 2015-10-21, release date: 2016-08-17, Last modification date: 2024-05-08)

Primary citation

Josts, I.,Almeida Hernandez, Y.,Andreeva, A.,Tidow, H.
Crystal Structure of a Group I Energy Coupling Factor Vitamin Transporter S Component in Complex with Its Cognate Substrate.
Cell Chem Biol, 23:827-836, 2016

PubMed Abstract: Energy coupling factor (ECF) transporters are responsible for the uptake of essential scarce nutrients in prokaryotes. This ATP-binding cassette transporter family comprises two subgroups that share a common architecture forming a tripartite membrane protein complex consisting of a translocation component and ATP hydrolyzing module and a substrate-capture (S) component. Here, we present the crystal structure of YkoE from Bacillus subtilis, the S component of the previously uncharacterized group I ECF transporter YkoEDC. Structural and biochemical analyses revealed the constituent residues of the thiamine-binding pocket as well as an unexpected mode of vitamin recognition. In addition, our experimental and bioinformatics data demonstrate major differences between YkoE and group II ECF transporters and indicate how group I vitamin transporter S components have diverged from other group I and group II ECF transporters.

PubMed: 27447050
DOI: 10.1016/j.chembiol.2016.06.008

Experimental method

X-RAY DIFFRACTION (1.95 Å)