Chaperonin complex with a newly folded protein encapsulated in the folding chamber

被引：0

作者：

D. K. Clare

P. J. Bakkes

H. van Heerikhuizen

S. M. van der Vies

H. R. Saibil

机构：

[1] Birkbeck College,Department of Crystallography and Institute for Structural and Molecular Biology

[2] Malet Street,Department of Pathology

[3] London WC1E 7HX,undefined

[4] UK,undefined

[5] VU University Medical Center,undefined

[6] De Boelelaan 1117,undefined

[7] 1081 HV Amsterdam,undefined

[8] The Netherlands,undefined

[9] Present address: Department of Molecular Microbiology,undefined

[10] Groningen Biomolecular Sciences and Biotechnology Institute,undefined

[11] University of Groningen,undefined

[12] Kerklaan 30,undefined

[13] 9751 NN Haren,undefined

[14] The Netherlands.,undefined

来源：

Nature | 2009年 / 457卷

关键词：

D O I：

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中图分类号：

学科分类号：

摘要：

In Escherichia coli the chaperonins GroEL and GroES form a double-ring complex that binds and folds nascent or unfolded proteins. The T4 bacteriophage has its own version of GroES, gp31, that forms a taller folding chamber to fold the major virus capsid protein, gp23. Clare et al. present the structure of gp23–chaperonin complexes showing gp23 encapsulated in the folding chamber. The folding chamber is distorted in order to enclose a large substrate. This is the first study to present an image of a newly folded protein just before its release from the GroEL folding chamber.

引用

页码：107 / 110

页数：3

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