RRC ID 32211
Author Lee Y, Nishizawa T, Yamashita K, Ishitani R, Nureki O.
Title Structural basis for the facilitative diffusion mechanism by SemiSWEET transporter.
Journal Nat Commun
Abstract SWEET family proteins mediate sugar transport across biological membranes and play crucial roles in plants and animals. The SWEETs and their bacterial homologues, the SemiSWEETs, are related to the PQ-loop family, which is characterized by highly conserved proline and glutamine residues (PQ-loop motif). Although the structures of the bacterial SemiSWEETs were recently reported, the conformational transition and the significance of the conserved motif in the transport cycle have remained elusive. Here we report crystal structures of SemiSWEET from Escherichia coli, in the both inward-open and outward-open states. A structural comparison revealed that SemiSWEET undergoes an intramolecular conformational change in each protomer. The conserved PQ-loop motif serves as a molecular hinge that enables the 'binder clip-like' motion of SemiSWEET. The present work provides the framework for understanding the overall transport cycles of SWEET and PQ-loop family proteins.
Volume 6
Pages 6112
Published 2015-1-19
DOI 10.1038/ncomms7112
PII ncomms7112
PMID 25598322
PMC PMC4309421
MeSH Biological Transport Crystallography, X-Ray Escherichia coli / metabolism* Escherichia coli Proteins / chemistry* Escherichia coli Proteins / metabolism* Membrane Transport Proteins / chemistry* Membrane Transport Proteins / metabolism* Protein Structure, Secondary Structure-Activity Relationship
IF 12.121
Times Cited 26
DNA material Genomic DNA of Escherichia coli JCM 20135 (JGD07547)
General Microbes