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2c7c

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Revision as of 04:24, 10 September 2015

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

Structural highlights

2c7c is a 21 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1aon, 1dk7, 1dkd, 1egs, 1fy9, 1fya, 1gr5, 1gr6, 1grl, 1gru, 1j4z, 1jon, 1kid, 1kp8, 1kpo, 1la1, 1mnf, 1oel, 1pcq, 1pf9, 1ss8, 1svt, 1sx3, 1sx4, 1xck, 2c7d, 2c7e
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600] [CH10_ECOLI] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from 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.

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^[1]

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

References

↑ Ranson NA, Clare DK, Farr GW, Houldershaw D, Horwich AL, Saibil HR. Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes. Nat Struct Mol Biol. 2006 Feb;13(2):147-52. Epub 2006 Jan 22. PMID:16429154 doi:10.1038/nsmb1046

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c7c"

@@ Line 2: / Line 2: @@
 <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>
+<table><tr><td colspan='2'>[[2c7c]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 id='related'><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 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=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>
+<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=2c7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7c OCA], [http://pdbe.org/2c7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c7c RCSB], [http://www.ebi.ac.uk/pdbsum/2c7c PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2c7c" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Bacillus coli migula 1895]]
 [[Category: Clare, D K]]
 [[Category: Farr, G W]]

2c7c

From Proteopedia

Revision as of 04:24, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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