2cgt
From Proteopedia
(New page: 200px<br /><applet load="2cgt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cgt" /> '''GROEL-ADP-GP31 COMPLEX'''<br /> ==Overview=...) |
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| - | [[Image:2cgt.gif|left|200px]]<br /><applet load="2cgt" size=" | + | [[Image:2cgt.gif|left|200px]]<br /><applet load="2cgt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cgt" /> | caption="2cgt" /> | ||
'''GROEL-ADP-GP31 COMPLEX'''<br /> | '''GROEL-ADP-GP31 COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with | + | 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== | ==About this Structure== | ||
| - | 2CGT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 2CGT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage 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== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bakkes, P | + | [[Category: Bakkes, P J.]] |
| - | [[Category: Clare, D | + | [[Category: Clare, D K.]] |
| - | [[Category: Heerikhuizen, H | + | [[Category: Heerikhuizen, H Van.]] |
| - | [[Category: Saibil, H | + | [[Category: Saibil, H R.]] |
| - | [[Category: Vies, S | + | [[Category: Vies, S M.Van Der.]] |
[[Category: capsid assembly]] | [[Category: capsid assembly]] | ||
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
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[[Category: groel]] | [[Category: groel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:29 2008'' |
Revision as of 14:48, 21 February 2008
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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 Bacteriophage 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
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