2cgt
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/2cgt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cgt RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CGT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ | + | 2CGT is a [[Protein complex]] structure of sequences 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]. |
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/16549073 16549073] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16549073 16549073] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: groel]] | [[Category: groel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:13 2008'' |
Revision as of 23:21, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GROEL-ADP-GP31 COMPLEX
Overview
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.
About this Structure
2CGT is a Protein complex structure of sequences from Enterobacteria phage t4 and Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 02:21:13 2008
