2c7c: Difference between revisions

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[[Image:~~2c7c~~.~~png~~|~~left~~|~~200px~~]]

==FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)==

== Structural highlights ==

<table><tr><td colspan='2'>[[2c7c]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C7C FirstGlance]. <br>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c7c RCSB], [http://www.ebi.ac.uk/pdbsum/2c7c PDBsum]</span></td></tr>

<table>

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/2c7c_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/chain_selection.php?pdb_ID=2ata ConSurf].

== Publication Abstract from PubMed ==

The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.

~~{{STRUCTURE_2c7c| PDB=2c7c | SCENE= }}~~

Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.,Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:16429154<ref>PMID:16429154</ref>

~~===FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_16429154}}~~

~~==About this Structure==~~

~~[[2c7c]] is~~ a ~~21 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann.ac.il/oca-bin~~/~~ocashort?id=2C7C OCA].~~

==See Also==

*[[Chaperonin|Chaperonin]]

*[[Heat Shock Proteins|Heat Shock Proteins]]

== References ==

==~~Reference~~==

<~~ref group="xtra">PMID:016429154<~~/~~ref~~><~~references group="xtra"~~/>

__TOC__

</StructureSection>

[[Category: Escherichia coli]]

[[Category: Clare, D K.]]

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-[[Image:2c7c.png|left|200px]]
+==FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)==
+<StructureSection load='2c7c' size='340' side='right' caption='[[2c7c]], [[Resolution|resolution]] 7.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2c7c]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C7C FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aon|1aon]], [[1dk7|1dk7]], [[1dkd|1dkd]], [[1egs|1egs]], [[1fy9|1fy9]], [[1fya|1fya]], [[1gr5|1gr5]], [[1gr6|1gr6]], [[1grl|1grl]], [[1gru|1gru]], [[1j4z|1j4z]], [[1jon|1jon]], [[1kid|1kid]], [[1kp8|1kp8]], [[1kpo|1kpo]], [[1la1|1la1]], [[1mnf|1mnf]], [[1oel|1oel]], [[1pcq|1pcq]], [[1pf9|1pf9]], [[1ss8|1ss8]], [[1svt|1svt]], [[1sx3|1sx3]], [[1sx4|1sx4]], [[1xck|1xck]], [[2c7d|2c7d]], [[2c7e|2c7e]]</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c7c RCSB], [http://www.ebi.ac.uk/pdbsum/2c7c PDBsum]</span></td></tr>
+<table>
+== 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/c7/2c7c_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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber, the so-called cis cavity. Upon ATP hydrolysis within the cis ring, the asymmetric complex becomes able to accept non-native polypeptides and ATP in the open, trans ring. Here we have examined the structural basis for this allosteric switch in activity by cryo-EM and single-particle image processing. ATP hydrolysis does not change the conformation of the cis ring, but its effects are transmitted through an inter-ring contact and cause domain rotations in the mobile trans ring. These rigid-body movements in the trans ring lead to disruption of its intra-ring contacts, expansion of the entire ring and opening of both the nucleotide pocket and the substrate-binding domains, admitting ATP and new substrate protein.
-{{STRUCTURE_2c7c|  PDB=2c7c  |  SCENE=  }}
+Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.,Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:16429154<ref>PMID:16429154</ref>
-===FITTED COORDINATES FOR GROEL-ATP7-GROES CRYO-EM COMPLEX (EMD-1180)===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_16429154}}
-==About this Structure==
-[[2c7c]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7C OCA].
 ==See Also==
 *[[Chaperonin|Chaperonin]]
 *[[Heat Shock Proteins|Heat Shock Proteins]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:016429154</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
 [[Category: Clare, D K.]]