3QNQ

Crystal structure of the transporter ChbC, the IIC component from the N,N'-diacetylchitobiose-specific phosphotransferase system

Summary for 3QNQ

• Entry DOI: 10.2210/pdb3qnq/pdb
• Related PRD ID: PRD_900001
• Descriptor: PTS system, cellobiose-specific IIC component, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: membrane protein, transporter, enzyme iic, phosphoenolpyruvate-sugar phosphotransferase system, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, hydrolase, transport protein
• Biological source: Bacillus cereus
• Total number of polymer chains: 4
• Total formula weight: 198734.88

Authors

Cao, Y.,Jin, X.,Huang, H.,Levin, E.J.,Zhou, M.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2011-02-08, release date: 2011-04-06, Last modification date: 2024-02-21)

Primary citation

Cao, Y.,Jin, X.,Levin, E.J.,Huang, H.,Zong, Y.,Quick, M.,Weng, J.,Pan, Y.,Love, J.,Punta, M.,Rost, B.,Hendrickson, W.A.,Javitch, J.A.,Rajashankar, K.R.,Zhou, M.
Crystal structure of a phosphorylation-coupled saccharide transporter.
Nature, 473:50-54, 2011

PubMed 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 His250 and Glu334 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.

PubMed: 21471968
DOI: 10.1038/nature09939

Experimental method

X-RAY DIFFRACTION (3.295 Å)