2cgt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_2cgt| PDB=2cgt | SCENE= }}
+
==GROEL-ADP-gp31 COMPLEX==
-
===GROEL-ADP-gp31 COMPLEX===
+
<StructureSection load='2cgt' size='340' side='right' caption='[[2cgt]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_16549073}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2cgt]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CGT FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aon|1aon]], [[1dk7|1dk7]], [[1dkd|1dkd]], [[1fy9|1fy9]], [[1fya|1fya]], [[1g31|1g31]], [[1gr5|1gr5]], [[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]], [[2c7c|2c7c]], [[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=2cgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cgt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cgt RCSB], [http://www.ebi.ac.uk/pdbsum/2cgt 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/cg/2cgt_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 ==
 +
Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to obtain three-dimensional structures of the E.coli chaperonin GroEL complexed with gp31, in the presence of both ATP and ADP. The GroEL-gp31-ADP map has a resolution of 8.2 A, which allows accurate fitting of the GroEL and gp31 crystal structures. Comparison of this fitted structure with that of the GroEL-GroES-ADP structure previously determined by cryo-electron microscopy shows that the folding cage is expanded. The enlarged volume for folding is consistent with the size of the bacteriophage coat protein gp23, which is the major substrate of GroEL-gp31 chaperonin complex. At 56 kDa, gp23 is close to the maximum size limit of a polypeptide that is thought to fit inside the GroEL-GroES folding cage.
-
==Function==
+
An expanded protein folding cage in the GroEL-gp31 complex.,Clare DK, Bakkes PJ, van Heerikhuizen H, van der Vies SM, Saibil HR J Mol Biol. 2006 May 5;358(3):905-11. Epub 2006 Mar 6. PMID:16549073<ref>PMID:16549073</ref>
-
[[http://www.uniprot.org/uniprot/CH60_ECOLI 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] [[http://www.uniprot.org/uniprot/VG31_BPT4 VG31_BPT4]] Essential for proper capsid assembly. In absence of Gp31 the major capsid protein (Gp23) assembles into 'lumps'. Acts as a co-chaperonin with the host groEL protein.
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[2cgt]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CGT OCA].
+
</div>
==See Also==
==See Also==
*[[Chaperonin|Chaperonin]]
*[[Chaperonin|Chaperonin]]
*[[Heat Shock Proteins|Heat Shock Proteins]]
*[[Heat Shock Proteins|Heat Shock Proteins]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:016549073</ref><references group="xtra"/><references/>
+
__TOC__
 +
</StructureSection>
[[Category: Enterobacteria phage t4]]
[[Category: Enterobacteria phage t4]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]

Revision as of 04:23, 3 October 2014

GROEL-ADP-gp31 COMPLEX

2cgt, resolution 8.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cgt"
Views
Personal tools
Navigation
Toolbox