2vv5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2vv5", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Current revision (15:33, 13 December 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2vv5.png|left|200px]]
 
-
<!--
+
==The open structure of MscS==
-
The line below this paragraph, containing "STRUCTURE_2vv5", creates the "Structure Box" on the page.
+
<StructureSection load='2vv5' size='340' side='right'caption='[[2vv5]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2vv5]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The November 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Mechanosensitive Channels'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_11 10.2210/rcsb_pdb/mom_2008_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VV5 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.45&#8491;</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=2vv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vv5 OCA], [https://pdbe.org/2vv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vv5 RCSB], [https://www.ebi.ac.uk/pdbsum/2vv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vv5 ProSAT]</span></td></tr>
-
{{STRUCTURE_2vv5| PDB=2vv5 | SCENE= }}
+
</table>
 +
== 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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vv/2vv5_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vv5 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia coli mechanosensitive channel, MscS, opens to allow rapid ion efflux, relieving the turgor pressure that would otherwise destroy the cell. We present a 3.45 angstrom-resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of approximately 13 angstroms created by substantial rotational rearrangement of the three transmembrane helices. The structure suggests a molecular mechanism that underlies MscS gating and its decay of conductivity during prolonged activation. Support for this mechanism is provided by single-channel analysis of mutants with altered gating characteristics.
-
===THE OPEN STRUCTURE OF MSCS===
+
The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution.,Wang W, Black SS, Edwards MD, Miller S, Morrison EL, Bartlett W, Dong C, Naismith JH, Booth IR Science. 2008 Aug 29;321(5893):1179-83. PMID:18755969<ref>PMID:18755969</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_18755969}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2vv5" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 18755969 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_18755969}}
+
-
 
+
-
==About this Structure==
+
-
[[2vv5]] is a 7 chain structure of [[Ion channels]] and [[Ion channels (Part II)]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The November 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Mechanosensitive Channels'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_11 10.2210/rcsb_pdb/mom_2008_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VV5 OCA].
+
==See Also==
==See Also==
-
*[[Ion channels|Ion channels]]
+
*[[Ion channels 3D structures|Ion channels 3D structures]]
-
*[[Ion channels (Part II)|Ion channels (Part II)]]
+
== References ==
-
*[[Mechanosensitive channels: opening and closing|Mechanosensitive channels: opening and closing]]
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
<ref group="xtra">PMID:018755969</ref><references group="xtra"/>
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
 +
[[Category: Large Structures]]
[[Category: Mechanosensitive Channels]]
[[Category: Mechanosensitive Channels]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
-
[[Category: Dong, C.]]
+
[[Category: Dong C]]
-
[[Category: Johnson, K A.]]
+
[[Category: Johnson KA]]
-
[[Category: Naismith, J H.]]
+
[[Category: Naismith JH]]
-
[[Category: Wang, W.]]
+
[[Category: Wang W]]
-
[[Category: Inner membrane]]
+
-
[[Category: Ion transport]]
+
-
[[Category: Ionic channel]]
+
-
[[Category: Membrane]]
+
-
[[Category: Membrane protein]]
+
-
[[Category: Membrane structure]]
+
-
[[Category: Open channel]]
+
-
[[Category: Transmembrane]]
+
-
[[Category: Transport]]
+

Current revision

The open structure of MscS

PDB ID 2vv5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools