5IWS

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

Summary for 5IWS

• Entry DOI: 10.2210/pdb5iws/pdb
• Related PRD ID: PRD_900001
• Descriptor: 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)
• Functional Keywords: transporter, membrane protein, structural genomics, new york consortium on membrane protein structure, nycomps, psi-biology, transferase
• Biological source: Bacillus cereus (strain ZK / E33L)
• Total number of polymer chains: 1
• Total formula weight: 52057.08

Authors

McCoy, J.G.,Ren, Z.,Levin, E.J.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2016-03-22, release date: 2016-05-25, Last modification date: 2020-07-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.551 Å)