2cgt
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(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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Revision as of 06:59, 21 November 2007
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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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