4hwa - Revision history

OCA at 11:46, 1 March 2024

OCA — Fri, 01 Mar 2024 11:46:32 GMT

←Older revision		Revision as of 11:46, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hwa]] 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=4HWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HWA FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hwa]] 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=4HWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HWA 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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [https://pdbe.org/4hwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [https://www.ebi.ac.uk/pdbsum/4hwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwa ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 4.37Å</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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [https://pdbe.org/4hwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [https://www.ebi.ac.uk/pdbsum/4hwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[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.		[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 ==
-	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 coliMscS are currently available, the wild type protein in a non-conducting state at 3.7 A resolution(Bass et al., Science 298, 1582 (2002)) and the Ala106Val variant in an open state at 3.45 A resolution (Wang et al., Science 321, 1179 (2008)). Both structures used protein solubilized in the detergent fos-choline-14. We report here crystal structures of MscS from Escherichia coli and Helicobacter pylori solubilized in the detergent beta-dodecylmaltoside (DDM) at resolutions of 4.4 and 4.2 A, respectively. While the cytoplasmic domains are unchanged in these structures, distinctconformations of the transmembrane domains are observed. Intriguingly, DDM solubilized wild type E. coliMscSadopts the open state structure of A106V E. coliMscS, while H. pyloriMscS resembles the non-conducting state structure observed for fos-choline-14 solubilized E. coliMscS. These results highlight the sensitivity of membrane protein conformational equilibria to variationsin detergent, crystallization conditions and protein sequence.
-
-	Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from E. coli and H. pylori at 4.4 A and 4.1 A resolution.,Lai JY, Poon YS, Kaiser JT, Rees DC Protein Sci. 2013 Jan 22. doi: 10.1002/pro.2222. PMID:23339071<ref>PMID:23339071</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4hwa" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Ion channels 3D structures\|Ion channels 3D structures]]		*[[Ion channels 3D structures\|Ion channels 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:19, 9 November 2022

OCA — Wed, 09 Nov 2022 08:19:09 GMT

←Older revision		Revision as of 08:19, 9 November 2022
Line 1:		Line 1:

	==Crystal Structure of Escherichia coli MscS Wildtype (Open State)==		==Crystal Structure of Escherichia coli MscS Wildtype (Open State)==
-	<StructureSection load='4hwa' size='340' side='right' caption='[[4hwa]], [[Resolution\|resolution]] 4.37Å' scene=''>	+	<StructureSection load='4hwa' size='340' side='right'caption='[[4hwa]], [[Resolution\|resolution]] 4.37Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hwa]] is a 7 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HWA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hwa]] 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=4HWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HWA FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vv5\|2vv5]], [[2oau\|2oau]], [[4hw9\|4hw9]]</td></tr>~~	+	</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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [https://pdbe.org/4hwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [https://www.ebi.ac.uk/pdbsum/4hwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwa ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2924, JW2891, mscS, yggB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [~~http~~://pdbe.org/4hwa PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hwa PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwa 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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:

	==See Also==		==See Also==
-	*[[Ion channels\|Ion channels]]	+	*[[Ion channels 3D structures\|Ion channels 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: ~~Kaiser, J~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Lai,~~ J Y]]	+	[[Category: Kaiser J]]
-	[[Category: ~~Poon, Y S~~]]	+	[[Category: Lai JY]]
-	[[Category: ~~Rees, D C~~]]	+	[[Category: Poon YS]]
-	[[Category: ~~Mechanosensitive channel]]~~	+	[[Category: Rees DC]]
-	~~[[Category: Membrane]]~~	+
-	~~[[Category: Membrane protein~~]]	+

OCA at 19:18, 5 August 2016

OCA — Fri, 05 Aug 2016 19:18:19 GMT

←Older revision		Revision as of 19:18, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Escherichia coli MscS Wildtype (Open State)==		==Crystal Structure of Escherichia coli MscS Wildtype (Open State)==
	<StructureSection load='4hwa' size='340' side='right' caption='[[4hwa]], [[Resolution\|resolution]] 4.37Å' scene=''>		<StructureSection load='4hwa' size='340' side='right' caption='[[4hwa]], [[Resolution\|resolution]] 4.37Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hwa]] is a 7 chain structure with sequence from [http://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=4HWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HWA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hwa]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HWA FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vv5\|2vv5]], [[2oau\|2oau]], [[4hw9\|4hw9]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vv5\|2vv5]], [[2oau\|2oau]], [[4hw9\|4hw9]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2924, JW2891, mscS, yggB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ~~Escherichia coli K-12~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2924, JW2891, mscS, yggB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [http://www.ebi.ac.uk/pdbsum/4hwa PDBsum]</span></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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [http://pdbe.org/4hwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [http://www.ebi.ac.uk/pdbsum/4hwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4hwa" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ion channels\|Ion channels]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli k-12~~]]	+	[[Category: Ecoli]]
	[[Category: Kaiser, J]]		[[Category: Kaiser, J]]
	[[Category: Lai, J Y]]		[[Category: Lai, J Y]]

OCA at 21:15, 25 December 2014

OCA — Thu, 25 Dec 2014 21:15:33 GMT

←Older revision		Revision as of 21:15, 25 December 2014
Line 7:		Line 7:
	<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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [http://www.ebi.ac.uk/pdbsum/4hwa PDBsum]</span></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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [http://www.ebi.ac.uk/pdbsum/4hwa PDBsum]</span></td></tr>
	</table>		</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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 13:04, 21 December 2014

OCA — Sun, 21 Dec 2014 13:04:36 GMT

←Older revision		Revision as of 13:04, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4hwa\| PDB=4hwa \| SCENE= }}~~	+	==Crystal Structure of Escherichia coli MscS Wildtype (Open State)==
-	===Crystal Structure of Escherichia coli MscS Wildtype (Open State)===	+	<StructureSection load='4hwa' size='340' side='right' caption='[[4hwa]], [[Resolution\|resolution]] 4.37Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23339071}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4hwa]] is a 7 chain structure with sequence from [http://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=4HWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HWA FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vv5\|2vv5]], [[2oau\|2oau]], [[4hw9\|4hw9]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">b2924, JW2891, mscS, yggB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=4hwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hwa RCSB], [http://www.ebi.ac.uk/pdbsum/4hwa PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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 coliMscS are currently available, the wild type protein in a non-conducting state at 3.7 A resolution(Bass et al., Science 298, 1582 (2002)) and the Ala106Val variant in an open state at 3.45 A resolution (Wang et al., Science 321, 1179 (2008)). Both structures used protein solubilized in the detergent fos-choline-14. We report here crystal structures of MscS from Escherichia coli and Helicobacter pylori solubilized in the detergent beta-dodecylmaltoside (DDM) at resolutions of 4.4 and 4.2 A, respectively. While the cytoplasmic domains are unchanged in these structures, distinctconformations of the transmembrane domains are observed. Intriguingly, DDM solubilized wild type E. coliMscSadopts the open state structure of A106V E. coliMscS, while H. pyloriMscS resembles the non-conducting state structure observed for fos-choline-14 solubilized E. coliMscS. These results highlight the sensitivity of membrane protein conformational equilibria to variationsin detergent, crystallization conditions and protein sequence.

-	~~==Function==~~	+	Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from E. coli and H. pylori at 4.4 A and 4.1 A resolution.,Lai JY, Poon YS, Kaiser JT, Rees DC Protein Sci. 2013 Jan 22. doi: 10.1002/pro.2222. PMID:23339071<ref>PMID:23339071</ref>
-	~~[[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~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4hwa]] is~~ a ~~7 chain structure with sequence from [http://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=4HWA OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023339071</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
-	[[Category: Kaiser, J.]]	+	[[Category: Kaiser, J]]
-	[[Category: Lai, J Y.]]	+	[[Category: Lai, J Y]]
-	[[Category: Poon, Y S.]]	+	[[Category: Poon, Y S]]
-	[[Category: Rees, D C.]]	+	[[Category: Rees, D C]]
	[[Category: Mechanosensitive channel]]		[[Category: Mechanosensitive channel]]
	[[Category: Membrane]]		[[Category: Membrane]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]

OCA at 09:34, 19 June 2013

OCA — Wed, 19 Jun 2013 09:34:54 GMT

←Older revision		Revision as of 09:34, 19 June 2013
Line 1:		Line 1:
-	[[Image:4hwa.jpg\|left\|200px]]
-
	{{STRUCTURE_4hwa\| PDB=4hwa \| SCENE= }}		{{STRUCTURE_4hwa\| PDB=4hwa \| SCENE= }}
-
	===Crystal Structure of Escherichia coli MscS Wildtype (Open State)===		===Crystal Structure of Escherichia coli MscS Wildtype (Open State)===
-
	{{ABSTRACT_PUBMED_23339071}}		{{ABSTRACT_PUBMED_23339071}}
		+
		+	==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.

	==About this Structure==		==About this Structure==
	[[4hwa]] is a 7 chain structure with sequence from [http://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=4HWA OCA].		[[4hwa]] is a 7 chain structure with sequence from [http://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=4HWA OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023339071</ref><references group="xtra"/><references/>
	[[Category: Escherichia coli k-12]]		[[Category: Escherichia coli k-12]]
	[[Category: Kaiser, J.]]		[[Category: Kaiser, J.]]

OCA at 10:29, 13 February 2013

OCA — Wed, 13 Feb 2013 10:29:21 GMT

←Older revision		Revision as of 10:29, 13 February 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4hwa.jpg\|left\|200px]]

-	~~The entry~~ 4hwa ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4hwa\| PDB=4hwa \| SCENE= }}

-	~~Authors: Lai, J.Y., Poon, Y.S., Kaiser, J., Rees, D.C.~~	+	===Crystal Structure of Escherichia coli MscS Wildtype (Open State)===

-	~~Description: Crystal~~ Structure of Escherichia coli ~~MscS Wildtype (Open State)~~	+	{{ABSTRACT_PUBMED_23339071}}
		+
		+	==About this Structure==
		+	[[4hwa]] is a 7 chain structure with sequence from [http://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=4HWA OCA].
		+	[[Category: Escherichia coli k-12]]
		+	[[Category: Kaiser, J.]]
		+	[[Category: Lai, J Y.]]
		+	[[Category: Poon, Y S.]]
		+	[[Category: Rees, D C.]]
		+	[[Category: Mechanosensitive channel]]
		+	[[Category: Membrane]]
		+	[[Category: Membrane protein]]

OCA at 11:06, 23 January 2013

OCA — Wed, 23 Jan 2013 11:06:43 GMT

←Older revision		Revision as of 11:06, 23 January 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4hwa is ON HOLD	+	The entry 4hwa is ON HOLD until Paper Publication

	Authors: Lai, J.Y., Poon, Y.S., Kaiser, J., Rees, D.C.		Authors: Lai, J.Y., Poon, Y.S., Kaiser, J., Rees, D.C.

	Description: Crystal Structure of Escherichia coli MscS Wildtype (Open State)		Description: Crystal Structure of Escherichia coli MscS Wildtype (Open State)

OCA at 09:08, 21 November 2012

OCA — Wed, 21 Nov 2012 09:08:10 GMT

←Older revision		Revision as of 09:08, 21 November 2012
Line 3:		Line 3:
	The entry 4hwa is ON HOLD		The entry 4hwa is ON HOLD

-	Authors: Lai, J.Y., Poon, Y.S., Kaiser, J, Rees, D.C.	+	Authors: Lai, J.Y., Poon, Y.S., Kaiser, J., Rees, D.C.

	Description: Crystal Structure of Escherichia coli MscS Wildtype (Open State)		Description: Crystal Structure of Escherichia coli MscS Wildtype (Open State)

OCA: Protected "4hwa" [edit=sysop:move=sysop]

OCA — Wed, 14 Nov 2012 06:20:54 GMT

Protected "4hwa" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:20, 14 November 2012