4KPT

Crystal structure of substrate binding domain 1 (SBD1) OF ABC transporter GLNPQ from lactococcus lactis

4KPT の概要

• エントリーDOI: 10.2210/pdb4kpt/pdb
• 関連するPDBエントリー: 4KQP 4KR5
• 分子名称: Glutamine ABC transporter permease and substrate binding protein protein, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, HEXAETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: glutamine binding protein, amino acid transport, transport protein, extracellular
• 由来する生物種: Lactococcus lactis subsp. lactis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57699.97

構造登録者

Vujicic Zagar, A.,Guskov, A.,Schuurman-Wolters, G.K.,Slotboom, D.J.,Poolman, B. (登録日: 2013-05-14, 公開日: 2013-09-11, 最終更新日: 2024-02-28)

主引用文献

Fulyani, F.,Schuurman-Wolters, G.K.,Zagar, A.V.,Guskov, A.,Slotboom, D.J.,Poolman, B.
Functional Diversity of Tandem Substrate-Binding Domains in ABC Transporters from Pathogenic Bacteria.
Structure, 21:1879-1888, 2013

PubMed Abstract: The ATP-binding cassette (ABC) transporter GlnPQ is an essential uptake system for amino acids in gram-positive pathogens and related nonpathogenic bacteria. The transporter has tandem substrate-binding domains (SBDs) fused to each transmembrane domain, giving rise to four SBDs per functional transporter complex. We have determined the crystal structures and ligand-binding properties of the SBDs of GlnPQ from Enterococcus faecalis, Streptococcus pneumoniae, and Lactococcus lactis. The tandem SBDs differ in substrate specificity and affinity, allowing cells to efficiently accumulate different amino acids via a single ABC transporter. The combined structural, functional, and thermodynamic analysis revealed the roles of individual residues in determining the substrate affinity. We succeeded in converting a low-affinity SBD into a high-affinity receptor and vice versa. Our data indicate that a small number of residues that reside in the binding pocket constitute the major affinity determinants of the SBDs.

PubMed: 23994008
DOI: 10.1016/j.str.2013.07.020

実験手法

X-RAY DIFFRACTION (1.4 Å)