Structural aspects of GroEL function

被引：55

作者：

Horovitz, A ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Struct, IL-76100 Rehovot, Israel

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 01期

基金：

以色列科学基金会;

关键词：

D O I：

10.1016/S0959-440X(98)80015-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The chaperonin GroEL and its cofactor GroES facilitate protein folding in an ATP-regulated manner. The recently solved crystal structure of the GroEL-GroES.(ADP)(7) complex shows that the lining of the cavity in the polypeptide acceptor state is hydrophobic, whereas in the protein-release state it becomes hydrophilic. Other highlights of the past year include the visualization of the allosteric states of GroEL with respect to ATP using cryo-electron microscopy, and an X-ray crystallographic analysis of the interaction between the apical domain of GroEL and a peptide.

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页码：93 / 100

页数：8

相关论文

共 76 条

[1] Inter-ring communication is disrupted in the GroEL mutant Arg13->Gly; Ala126->Val with known crystal structure [J].

Aharoni, A ;

Horovitz, A .

JOURNAL OF MOLECULAR BIOLOGY, 1996, 258 (05) :732-735

[2] Detection of changes in pairwise interactions during allosteric transitions: Coupling between local and global conformational changes in GroEL [J].

Aharoni, A ;

Horovitz, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (05) :1698-1702

[3] Refolding chromatography with immobilized mini-chaperones [J].

Altamirano, MM ;

Golbik, R ;

Zahn, R ;

Buckle, AM ;

Fersht, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (08) :3576-3578

[4] The protein-folding activity of chaperonins correlates with the symmetric GroEL(14)(GroES(7))(2) heterooligomer [J].

Azem, A ;

Diamant, S ;

Kessel, M ;

Weiss, C ;

Goloubinoff, P .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (26) :12021-12025

[5] Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions [J].

Behlke, J ;

Ristau, O ;

Schonfeld, HJ .

BIOCHEMISTRY, 1997, 36 (17) :5149-5156

[6]

BOCHKAREVA ES, 1992, J BIOL CHEM, V267, P6796

[7] The 2.4 angstrom crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S [J].

Boisvert, DC ;

Wang, JM ;

Otwinowski, Z ;

Horwich, AL ;

Sigler, PB .

NATURE STRUCTURAL BIOLOGY, 1996, 3 (02) :170-177

[8] THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J].

BRAIG, K ;

OTWINOWSKI, Z ;

HEGDE, R ;

BOISVERT, DC ;

JOACHIMIAK, A ;

HORWICH, AL ;

SIGLER, PB .

NATURE, 1994, 371 (6498) :578-586

[9] CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION [J].

BRAIG, K ;

ADAMS, PD ;

BRUNGER, AT .

NATURE STRUCTURAL BIOLOGY, 1995, 2 (12) :1083-1094

[10] A structural model for GroEL-polypeptide recognition [J].

Buckle, AM ;

Zahn, R ;

Fersht, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (08) :3571-3575

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