Crystal Structure of a Phosphorylation-coupled Saccharide Transporter

Overview

Journal Nature

Specialty Science

Date 2011 Apr 8

PMID 21471968

Citations 35

Authors

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

Ming Zhou

Affiliations

Soon will be listed here.

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.

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