2cgt

From Proteopedia

(Difference between revisions)

Revision as of 16:49, 10 April 2020

GROEL-ADP-gp31 COMPLEX

2cgt, resolution 8.20Å

Structural highlights

2cgt is a 21 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Bpt4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1aon, 1dk7, 1dkd, 1fy9, 1fya, 1g31, 1gr5, 1grl, 1gru, 1j4z, 1jon, 1kid, 1kp8, 1kpo, 1la1, 1mnf, 1oel, 1pcq, 1pf9, 1ss8, 1svt, 1sx3, 1sx4, 1xck, 2c7c, 2c7d, 2c7e
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [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.

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[1]

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

References

↑ Clare DK, Bakkes PJ, van Heerikhuizen H, van der Vies SM, Saibil HR. An expanded protein folding cage in the GroEL-gp31 complex. J Mol Biol. 2006 May 5;358(3):905-11. Epub 2006 Mar 6. PMID:16549073 doi:10.1016/j.jmb.2006.02.033

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/2cgt"

@@ Line 3: / Line 3: @@
 <SX load='2cgt' size='340' side='right' viewer='molstar' caption='[[2cgt]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cgt]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. 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>
+<table><tr><td colspan='2'>[[2cgt]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. 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://proteopedia.org/fgij/fg.htm?mol=2CGT 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]], [[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 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=2cgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cgt OCA], [http://pdbe.org/2cgt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cgt RCSB], [http://www.ebi.ac.uk/pdbsum/2cgt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cgt ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2cgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cgt OCA], [http://pdbe.org/2cgt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cgt RCSB], [http://www.ebi.ac.uk/pdbsum/2cgt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cgt ProSAT]</span></td></tr>
 </table>
 == Function ==

2cgt

From Proteopedia

Revision as of 16:49, 10 April 2020

GROEL-ADP-gp31 COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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