4DVE

Crystal structure at 2.1 A of the S-component for biotin from an ECF-type ABC transporter

4DVE の概要

• エントリーDOI: 10.2210/pdb4dve/pdb
• 分子名称: Biotin transporter BioY, BIOTIN, nonyl beta-D-glucopyranoside, ... (4 entities in total)
• 機能のキーワード: ecf-transport, ligand-binding domain, biotin binding, membrane, transport protein
• 由来する生物種: Lactococcus lactis subsp. cremoris
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Probable): A2RMJ9
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 68428.26

構造登録者

Berntsson, R.P.-A.,ter Beek, J.,Majsnerowska, M.,Duurkens, R.,Puri, P.,Poolman, B.,Slotboom, D.J. (登録日: 2012-02-23, 公開日: 2012-08-29, 最終更新日: 2024-11-20)

主引用文献

Berntsson, R.P.,Ter Beek, J.,Majsnerowska, M.,Duurkens, R.H.,Puri, P.,Poolman, B.,Slotboom, D.J.
Structural divergence of paralogous S components from ECF-type ABC transporters.
Proc.Natl.Acad.Sci.USA, 109:13990-13995, 2012

PubMed Abstract: Energy coupling factor (ECF) proteins are ATP-binding cassette transporters involved in the import of micronutrients in prokaryotes. They consist of two nucleotide-binding subunits and the integral membrane subunit EcfT, which together form the ECF module and a second integral membrane subunit that captures the substrate (the S component). Different S components, unrelated in sequence and specific for different ligands, can interact with the same ECF module. Here, we present a high-resolution crystal structure at 2.1 Å of the biotin-specific S component BioY from Lactococcus lactis. BioY shares only 16% sequence identity with the thiamin-specific S component ThiT from the same organism, of which we recently solved a crystal structure. Consistent with the lack of sequence similarity, BioY and ThiT display large structural differences (rmsd = 5.1 Å), but the divergence is not equally distributed over the molecules: The S components contain a structurally conserved N-terminal domain that is involved in the interaction with the ECF module and a highly divergent C-terminal domain that binds the substrate. The domain structure explains how the S components with large overall structural differences can interact with the same ECF module while at the same time specifically bind very different substrates with subnanomolar affinity. Solitary BioY (in the absence of the ECF module) is monomeric in detergent solution and binds D-biotin with a high affinity but does not transport the substrate across the membrane.

PubMed: 22891302
DOI: 10.1073/pnas.1203219109

実験手法

X-RAY DIFFRACTION (2.09 Å)