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Title: The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport

Journal Article · · Structure
 [1];  [2];  [2];  [3];  [2];  [2];  [4];  [5];  [3];  [2]
  1. Baylor College of Medicine, Houston, TX (United States); Broad Inst., Cambridge, MA (United States)
  2. Baylor College of Medicine, Houston, TX (United States)
  3. Univ. of Kansas, Lawrence, KS (United States)
  4. College of Staten Island, Staten Island, NY (United States)
  5. Columbia Univ., New York, NY (United States)

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. Furthermore, these results provide a mechanistic framework for understanding substrate recognition and translocation for the glucose superfamily EIIC transporters.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
National Institutes of Health (NIH); American Heart Assoc.; Cancer Prevention and Research Institute of Texas; National Inst. of General Medical Sciences
Grant/Contract Number:
R01GM098878; R01HL086392; R01DK088057; U54GM095315; U54GM087519; 12EIA8850017; R1223; P41 GM103403
OSTI ID:
1257484
Journal Information:
Structure, Vol. 24, Issue 6; ISSN 0969-2126
Publisher:
ElsevierCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 29 works
Citation information provided by
Web of Science

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Cited By (5)

Transporter oligomerisation: roles in structure and function journal December 2018
Thermodynamics of voltage-gated ion channels journal November 2018
Inward-facing conformation of l-ascorbate transporter suggests an elevator mechanism journal July 2018
Difference distance map data of alternative crystal forms of UlaA journal February 2017
Substituted cysteine accessibility method (SCAM) analysis of the transport domain of human concentrative nucleoside transporter 3 (hCNT3) and other family members reveals features of structural and functional importance journal July 2017

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