4HWA: Crystal Structure Of Escherichia Coli Mscs Wildtype (open State)

The mechanosensitive channel of small conductance (MscS) contributes to the survival of bacteria during osmotic downshock by transiently opening large diameter pores for the efflux of cellular contents before the membrane ruptures. Two crystal structures of the Escherichia coli MscS are currently available, the wild type protein in a nonconducting state at 3.7 A resolution (Bass et al., Science 2002; 298:1582-1587) and the Ala106Val variant in an open state at 3.45 A resolution (Wang et al., Science 2008; 321:1179-1183). Both structures used protein solubilized in the detergent fos-choline-14. We report here crystal structures of MscS from E. coli and Helicobacter pylori solubilized in the detergent beta-dodecylmaltoside at resolutions of 4.4 and 4.2 A, respectively. While the cytoplasmic domains are unchanged in these structures, distinct conformations of the transmembrane domains are observed. Intriguingly, beta-dodecylmaltoside solubilized wild type E. coli MscS adopts the open state structure of A106V E. coli MscS, while H. pylori MscS resembles the nonconducting state structure observed for fos-choline-14 solubilized E. coli MscS. These results highlight the sensitivity of membrane protein conformational equilibria to variations in detergent, crystallization conditions, and protein sequence.
PDB ID: 4HWADownload
MMDB ID: 107625
PDB Deposition Date: 2012/11/7
Updated in MMDB: 2013/06
Experimental Method:
x-ray diffraction
Resolution: 4.37  Å
Source Organism:
Similar Structures:
Biological Unit for 4HWA: heptameric; determined by author and by software (PISA)
Molecular Components in 4HWA
Label Count Molecule
Proteins (7 molecules)
Small-conductance Mechanosensitive Channel(Gene symbol: mscS)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB