5IWS

Crystal structure of the transporter MalT, the EIIC domain from the maltose-specific phosphotransferase system

5IWS の概要

• エントリーDOI: 10.2210/pdb5iws/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Protein-N(Pi)-phosphohistidine-sugar phosphotransferase (Enzyme II of the phosphotransferase system) (PTS system glucose-specific IIBC component), alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: transporter, membrane protein, structural genomics, new york consortium on membrane protein structure, nycomps, psi-biology, transferase
• 由来する生物種: Bacillus cereus (strain ZK / E33L)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52057.08

構造登録者

McCoy, J.G.,Ren, Z.,Levin, E.J.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (登録日: 2016-03-22, 公開日: 2016-05-25, 最終更新日: 2024-11-20)

主引用文献

McCoy, J.G.,Ren, Z.,Stanevich, V.,Lee, J.,Mitra, S.,Levin, E.J.,Poget, S.,Quick, M.,Im, W.,Zhou, M.
The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport.
Structure, 24:956-964, 2016

PubMed Abstract: The phosphoenolpyruvate:carbohydrate phosphotransferase systems are found in bacteria, where they play central roles in sugar uptake and regulation of cellular uptake processes. Little is known about how the membrane-embedded components (EIICs) selectively mediate the passage of carbohydrates across the membrane. Here we report the functional characterization and 2.55-Å resolution structure of a maltose transporter, bcMalT, belonging to the glucose superfamily of EIIC transporters. bcMalT crystallized in an outward-facing occluded conformation, in contrast to the structure of another glucose superfamily EIIC, bcChbC, which crystallized in an inward-facing occluded conformation. The structures differ in the position of a structurally conserved substrate-binding domain that is suggested to play a central role in sugar transport. In addition, molecular dynamics simulations suggest a potential pathway for substrate entry from the periplasm into the bcMalT substrate-binding site. These results provide a mechanistic framework for understanding substrate recognition and translocation for the glucose superfamily EIIC transporters.

PubMed: 27161976
DOI: 10.1016/j.str.2016.04.003

実験手法

X-RAY DIFFRACTION (2.551 Å)