1kyk: Difference between revisions
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[[ | ==HOMOLOGY MODEL OF THE MECHANOSENSITIVE CHANNEL FROM ESCHERICHIA COLI: A CLOSED STATE== | ||
<StructureSection load='1kyk' size='340' side='right'caption='[[1kyk]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KYK FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kyk FirstGlance], [https://www.ebi.ac.uk/pdbsum/1kyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kyk ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mechanosensitive channels act as membrane-embedded mechano-electrical switches, opening a large water-filled pore in response to lipid bilayer deformations. This process is critical to the response of living organisms to direct physical stimulation, such as in touch, hearing and osmoregulation. Here, we have determined the structural rearrangements that underlie these events in the large prokaryotic mechanosensitive channel (MscL) using electron paramagnetic resonance spectroscopy and site-directed spin labelling. MscL was trapped in both the open and in an intermediate closed state by modulating bilayer morphology. Transition to the intermediate state is characterized by small movements in the first transmembrane helix (TM1). Subsequent transitions to the open state are accompanied by massive rearrangements in both TM1 and TM2, as shown by large increases in probe dynamics, solvent accessibility and the elimination of all intersubunit spin-spin interactions. The open state is highly dynamic, supporting a water-filled pore of at least 25 A, lined mostly by TM1. These structures suggest a plausible molecular mechanism of gating in mechanosensitive channels. | |||
Open channel structure of MscL and the gating mechanism of mechanosensitive channels.,Perozo E, Cortes DM, Sompornpisut P, Kloda A, Martinac B Nature. 2002 Aug 29;418(6901):942-8. PMID:12198539<ref>PMID:12198539</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kyk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
== | [[Category: Cortes, D M]] | ||
[[Category: Koda, A]] | |||
[[Category: Martinac, B]] | |||
== | [[Category: Perozo, E]] | ||
< | [[Category: Sompornpisut, P]] | ||
Latest revision as of 09:37, 18 August 2021
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HOMOLOGY MODEL OF THE MECHANOSENSITIVE CHANNEL FROM ESCHERICHIA COLI: A CLOSED STATEHOMOLOGY MODEL OF THE MECHANOSENSITIVE CHANNEL FROM ESCHERICHIA COLI: A CLOSED STATE
Structural highlights
Publication Abstract from PubMedMechanosensitive channels act as membrane-embedded mechano-electrical switches, opening a large water-filled pore in response to lipid bilayer deformations. This process is critical to the response of living organisms to direct physical stimulation, such as in touch, hearing and osmoregulation. Here, we have determined the structural rearrangements that underlie these events in the large prokaryotic mechanosensitive channel (MscL) using electron paramagnetic resonance spectroscopy and site-directed spin labelling. MscL was trapped in both the open and in an intermediate closed state by modulating bilayer morphology. Transition to the intermediate state is characterized by small movements in the first transmembrane helix (TM1). Subsequent transitions to the open state are accompanied by massive rearrangements in both TM1 and TM2, as shown by large increases in probe dynamics, solvent accessibility and the elimination of all intersubunit spin-spin interactions. The open state is highly dynamic, supporting a water-filled pore of at least 25 A, lined mostly by TM1. These structures suggest a plausible molecular mechanism of gating in mechanosensitive channels. Open channel structure of MscL and the gating mechanism of mechanosensitive channels.,Perozo E, Cortes DM, Sompornpisut P, Kloda A, Martinac B Nature. 2002 Aug 29;418(6901):942-8. PMID:12198539[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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