6pwp - Revision history

OCA at 09:27, 20 March 2024

OCA — Wed, 20 Mar 2024 09:27:48 GMT

←Older revision		Revision as of 09:27, 20 March 2024
Line 3:		Line 3:
	<SX load='6pwp' size='340' side='right' viewer='molstar' caption='[[6pwp]], [[Resolution\|resolution]] 4.10Å' scene=''>		<SX load='6pwp' size='340' side='right' viewer='molstar' caption='[[6pwp]], [[Resolution\|resolution]] 4.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6pwp]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6PWP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6pwp]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PWP FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6pwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwp OCA], [~~http~~://pdbe.org/6pwp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6pwp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6pwp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwp ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 4.1Å</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=6pwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwp OCA], [https://pdbe.org/6pwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pwp RCSB], [https://www.ebi.ac.uk/pdbsum/6pwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MSCS_ECOLI MSCS_ECOLI]] Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds. The channel pore is formed by TM3 and the loop between TM2 and TM3. After a sharp turn at Gly-113, an alpha-helix (residues 114-127) is oriented nearly parallel to the plane of the putative lipid bilayer. On the intracellular side of the channel, the permeation pathway of MscS does not connect directly to the cytoplasm but instead opens to a large chamber that is connected to the cytoplasm. This chamber resembles a molecular filter that could serve to prescreen large molecules before they are allowed passage to the transmembrane pore. The TM1 and TM2 helices appear to be likely candidates for mediating the tension and voltage sensitivities of MscS. Gating requires large rearrangements of at least the C-terminus.	+	[https://www.uniprot.org/uniprot/MSCS_ECOLI MSCS_ECOLI] Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds. The channel pore is formed by TM3 and the loop between TM2 and TM3. After a sharp turn at Gly-113, an alpha-helix (residues 114-127) is oriented nearly parallel to the plane of the putative lipid bilayer. On the intracellular side of the channel, the permeation pathway of MscS does not connect directly to the cytoplasm but instead opens to a large chamber that is connected to the cytoplasm. This chamber resembles a molecular filter that could serve to prescreen large molecules before they are allowed passage to the transmembrane pore. The TM1 and TM2 helices appear to be likely candidates for mediating the tension and voltage sensitivities of MscS. Gating requires large rearrangements of at least the C-terminus.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Prokaryotic mechanosensitive (MS) channels open by sensing the physical state of the membrane. As such, lipid-protein interactions represent the defining molecular process underlying mechanotransduction. Here, we describe cryo-electron microscopy (cryo-EM) structures of the E. coli small-conductance mechanosensitive channel (MscS) in nanodiscs (ND). They reveal a novel membrane-anchoring fold that plays a significant role in channel activation and establish a new location for the lipid bilayer, shifted ~14 A from previous consensus placements. Two types of lipid densities are explicitly observed. A phospholipid that 'hooks' the top of each TM2-TM3 hairpin and likely plays a role in force sensing, and a bundle of acyl chains occluding the permeation path above the L105 cuff. These observations reshape our understanding of force-from-lipids gating in MscS and highlight the key role of allosteric interactions between TM segments and phospholipids bound to key dynamic components of the channel.	+

-	Molecular basis of force-from-lipids gating in the mechanosensitive channel MscS.,Reddy B, Bavi N, Lu A, Park Y, Perozo E Elife. 2019 Dec 27;8. pii: 50486. doi: 10.7554/eLife.50486. PMID:31880537<ref>PMID:31880537</ref>	+	==See Also==
-		+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6pwp" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</SX>		</SX>
		+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Perozo, E]]	+	[[Category: Perozo E]]
-	[[Category: Reddy~~, B G]]~~	+	[[Category: Reddy BG]]
-	~~[[Category: Channel]]~~	+
-	~~[[Category: Mechanosensitive]]~~	+
-	~~[[Category: Mechanosensitive channel of small conductance]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Msc]]~~	+
-	~~[[Category: Nanodisc~~]]	+

OCA at 04:41, 11 April 2020

OCA — Sat, 11 Apr 2020 04:41:32 GMT

←Older revision		Revision as of 04:41, 11 April 2020
Line 3:		Line 3:
	<SX load='6pwp' size='340' side='right' viewer='molstar' caption='[[6pwp]], [[Resolution\|resolution]] 4.10Å' scene=''>		<SX load='6pwp' size='340' side='right' viewer='molstar' caption='[[6pwp]], [[Resolution\|resolution]] 4.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6pwp]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWP OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6PWP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6pwp]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6PWP FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6pwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwp OCA], [http://pdbe.org/6pwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pwp RCSB], [http://www.ebi.ac.uk/pdbsum/6pwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwp ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6pwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwp OCA], [http://pdbe.org/6pwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pwp RCSB], [http://www.ebi.ac.uk/pdbsum/6pwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 23:28, 6 March 2020

OCA — Fri, 06 Mar 2020 23:28:34 GMT

←Older revision		Revision as of 23:28, 6 March 2020
Line 1:		Line 1:

	==MscS Nanodisc==		==MscS Nanodisc==
-	<~~StructureSection~~ load='6pwp' size='340' side='right'caption='[[6pwp]], [[Resolution\|resolution]] 4.10Å' scene=''>	+	<SX load='6pwp' size='340' side='right' viewer='molstar' caption='[[6pwp]], [[Resolution\|resolution]] 4.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6pwp]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PWP FirstGlance]. <br>		<table><tr><td colspan='2'>[[6pwp]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PWP FirstGlance]. <br>
Line 20:		Line 20:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Perozo, E]]		[[Category: Perozo, E]]

OCA at 07:37, 8 January 2020

OCA — Wed, 08 Jan 2020 07:37:59 GMT

←Older revision		Revision as of 07:37, 8 January 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6pwp is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==MscS Nanodisc==
		+	<StructureSection load='6pwp' size='340' side='right'caption='[[6pwp]], [[Resolution\|resolution]] 4.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6pwp]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PWP FirstGlance]. <br>
		+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pwp OCA], [http://pdbe.org/6pwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pwp RCSB], [http://www.ebi.ac.uk/pdbsum/6pwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pwp ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MSCS_ECOLI MSCS_ECOLI]] Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage; as the membrane is depolarized, less tension is required to open the channel and vice versa. The channel is characterized by short bursts of activity that last for a few seconds. The channel pore is formed by TM3 and the loop between TM2 and TM3. After a sharp turn at Gly-113, an alpha-helix (residues 114-127) is oriented nearly parallel to the plane of the putative lipid bilayer. On the intracellular side of the channel, the permeation pathway of MscS does not connect directly to the cytoplasm but instead opens to a large chamber that is connected to the cytoplasm. This chamber resembles a molecular filter that could serve to prescreen large molecules before they are allowed passage to the transmembrane pore. The TM1 and TM2 helices appear to be likely candidates for mediating the tension and voltage sensitivities of MscS. Gating requires large rearrangements of at least the C-terminus.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Prokaryotic mechanosensitive (MS) channels open by sensing the physical state of the membrane. As such, lipid-protein interactions represent the defining molecular process underlying mechanotransduction. Here, we describe cryo-electron microscopy (cryo-EM) structures of the E. coli small-conductance mechanosensitive channel (MscS) in nanodiscs (ND). They reveal a novel membrane-anchoring fold that plays a significant role in channel activation and establish a new location for the lipid bilayer, shifted ~14 A from previous consensus placements. Two types of lipid densities are explicitly observed. A phospholipid that 'hooks' the top of each TM2-TM3 hairpin and likely plays a role in force sensing, and a bundle of acyl chains occluding the permeation path above the L105 cuff. These observations reshape our understanding of force-from-lipids gating in MscS and highlight the key role of allosteric interactions between TM segments and phospholipids bound to key dynamic components of the channel.

-	~~Authors: Reddy~~, B~~.G.~~, ~~Perozo~~, E.	+	Molecular basis of force-from-lipids gating in the mechanosensitive channel MscS.,Reddy B, Bavi N, Lu A, Park Y, Perozo E Elife. 2019 Dec 27;8. pii: 50486. doi: 10.7554/eLife.50486. PMID:31880537<ref>PMID:31880537</ref>

-	~~Description~~: ~~MscS Nanodisc~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6pwp" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Perozo, E]]		[[Category: Perozo, E]]
-	[[Category: Reddy, B.G]]	+	[[Category: Reddy, B G]]
		+	[[Category: Channel]]
		+	[[Category: Mechanosensitive]]
		+	[[Category: Mechanosensitive channel of small conductance]]
		+	[[Category: Membrane protein]]
		+	[[Category: Msc]]
		+	[[Category: Nanodisc]]

OCA at 05:11, 27 November 2019

OCA — Wed, 27 Nov 2019 05:11:03 GMT

←Older revision		Revision as of 05:11, 27 November 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6pwp is ON HOLD	+	The entry 6pwp is ON HOLD until Paper Publication

	Authors: Reddy, B.G., Perozo, E.		Authors: Reddy, B.G., Perozo, E.

OCA: Protected "6pwp" [edit=sysop:move=sysop]

OCA — Wed, 31 Jul 2019 04:49:58 GMT

Protected "6pwp" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:49, 31 July 2019

OCA: New page: '''Unreleased structure''' The entry 6pwp is ON HOLD Authors: Reddy, B.G., Perozo, E. Description: MscS Nanodisc Category: Unreleased Structures Category: Perozo, E [[Category:...

OCA — Wed, 31 Jul 2019 04:49:57 GMT

New page: '''Unreleased structure''' The entry 6pwp is ON HOLD Authors: Reddy, B.G., Perozo, E. Description: MscS Nanodisc Category: Unreleased Structures Category: Perozo, E [[Category:...

New page

'''Unreleased structure'''

The entry 6pwp is ON HOLD

Authors: Reddy, B.G., Perozo, E.

Description: MscS Nanodisc
[[Category: Unreleased Structures]]
[[Category: Perozo, E]]
[[Category: Reddy, B.G]]