Crystal structure of a phosphorylation-coupled saccharide transporter

Yu Cao, Xiangshu Jin, Elena J. Levin, Hua Huang, Yinong Zong, Matthias Quick, Jun Weng, Yaping Pan, James Love, Marco Punta, Burkhard Rost, Wayne A. Hendrickson, Jonathan A. Javitch, Kanagalaghatta R. Rajashankar and Ming Zhou ()
Additional contact information
Yu Cao: College of Physicians and Surgeons, Columbia University
Xiangshu Jin: Center for Computational Biology and Bioinformatics, Howard Hughes Medical Institute, Columbia University
Elena J. Levin: College of Physicians and Surgeons, Columbia University
Hua Huang: College of Physicians and Surgeons, Columbia University
Yinong Zong: Sanford-Burnham Institute
Matthias Quick: Columbia University
Jun Weng: College of Physicians and Surgeons, Columbia University
Yaping Pan: College of Physicians and Surgeons, Columbia University
James Love: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Marco Punta: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Burkhard Rost: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Wayne A. Hendrickson: New York Consortium on Membrane Protein Structure, New York Structural Biology Center
Jonathan A. Javitch: Columbia University
Kanagalaghatta R. Rajashankar: Cornell University, NE-CAT, Advanced Photon Source
Ming Zhou: College of Physicians and Surgeons, Columbia University

Nature, 2011, vol. 473, issue 7345, 50-54

Abstract: Abstract Saccharides have a central role in the nutrition of all living organisms. Whereas several saccharide uptake systems are shared between the different phylogenetic kingdoms, the phosphoenolpyruvate-dependent phosphotransferase system exists almost exclusively in bacteria. This multi-component system includes an integral membrane protein EIIC that transports saccharides and assists in their phosphorylation. Here we present the crystal structure of an EIIC from Bacillus cereus that transports diacetylchitobiose. The EIIC is a homodimer, with an expansive interface formed between the amino-terminal halves of the two protomers. The carboxy-terminal half of each protomer has a large binding pocket that contains a diacetylchitobiose, which is occluded from both sides of the membrane with its site of phosphorylation near the conserved His 250 and Glu 334 residues. The structure shows the architecture of this important class of transporters, identifies the determinants of substrate binding and phosphorylation, and provides a framework for understanding the mechanism of sugar translocation.

Date: 2011
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DOI: 10.1038/nature09939

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