한빛사논문
- 조회5,226
Abstract
1 School of Medical Sciences, University of Aberdeen, Institute of Medical Sciences, Foresterhill, Aberdeen, AB25 2ZD, UK.
2 Department of Physiology, University of Texas, Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-9040, USA.
3 UCLA-DOE Center for Genomics and Proteomics, University of California Los Angeles, 611 Charles E. Young Drive E., Los Angeles, California 90095−1570, USA.
4 These authors contributed equally to this work.
Correspondence should be addressed to Ian R BoothThe crystal structure of an open form of the Escherichia coli MscS mechanosensitive channel was recently solved. However, the conformation of the closed state and the gating transition remain uncharacterized. The pore-lining transmembrane helix contains a conserved glycine- and alanine-rich motif that forms a helix-helix interface. We show that introducing \''knobs\'' on the smooth glycine face by replacing glycine with alanine, and substituting conserved alanines with larger residues, increases the pressure required for gating. Creation of a glycine-glycine interface lowers activation pressure. The importance of residues Gly104, Ala106 and Gly108, which flank the hydrophobic seal, is demonstrated. A new structural model is proposed for the closed-to-open transition that involves rotation and tilt of the pore-lining helices. Introduction of glycine at Ala106 validated this model by acting as a powerful suppressor of defects seen with mutations at Gly104 and Gly108.
논문정보
- Research article
- 2005년 01월 (BRIC 등록일 )
- 국외 연구진
- 생명과학 > 유전학
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