Structure of an Open Form of an E. coli Mechanosensitive Channel at 3.45 Å Resolution

• Published in: Science (American Association for the Advancement of Science) Vol. 321; no. 5893; pp. 1179 - 1183
• Main Authors: Wang, Wenjian, Black, Susan S, Edwards, Michelle D, Miller, Samantha, Morrison, Emma L, Bartlett, Wendy, Dong, Changjiang, Naismith, James H, Booth, Ian R
• Format: Journal Article
• Language: English
• Published: Washington, DC American Association for the Advancement of Science 29.08.2008
• Subjects: Biological and medical sciences; Cell Membrane - chemistry; Crystal structure; Crystallography, X-Ray; Electric Conductivity; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - physiology; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - physiology; Free energy; Fundamental and applied biological sciences. Psychology; Hydrophobic and Hydrophilic Interactions; Ion Channel Gating; Ion channels; Ion Channels - chemistry; Ion Channels - genetics; Ion Channels - physiology; Kinetics; Microbiology; Modeling; Models, Molecular; Molecules; Monomers; Morphology, structure, chemical composition, physicochemical properties; Mutant Proteins - chemistry; mutants; Mutation; P branes; Patch-Clamp Techniques; Pressure; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Research Article; String theory; turgor; Vapors; Virology; Three dimensional structure; Molecular structure; Escherichia coli; Bacteria; Ionic channel; Membrane channel; Enterobacteriaceae; Conformation

How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia coli mechanosensitive channel, MscS, opens to allow rapid ion efflux, relieving the turgor pressure that would otherwise destroy the cell. We present a 3.45 angstrom-resolution str...