The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutation-ally defined functional sites on the channel walls and its outward imaginations, and at the ends of the cylinder.

[1]  K. Wüthrich,et al.  Destabilization of the complete protein secondary structure on binding to the chaperone GroEL , 1994, Nature.

[2]  Randy J. Read,et al.  Improved Fourier Coefficients for Maps Using Phases from Partial Structures with Errors , 1986 .

[3]  F. Hartl,et al.  A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1 , 1991, Nature.

[4]  Ellis Rj.  Protein folding. Chaperonin duet. , 1993 .

[5]  D. Eisenberg,et al.  Assessment of protein models with three-dimensional profiles , 1992, Nature.

[6]  S. Miller.  The structure of interfaces between subunits of dimeric and tetrameric proteins. , 1989, Protein engineering.

[7]  L. Gierasch,et al.  Different conformations for the same polypeptide bound to chaperones DnaK and GroEL , 1992, Nature.

[8]  K. Furtak,et al.  Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL , 1993, Cell.

[9]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[10]  K. Braig,et al.  A polypeptide bound by the chaperonin groEL is localized within a central cavity. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[11]  T. Creighton,et al.  Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha‐lactalbumin. , 1994, The EMBO journal.

[12]  W. Baumeister,et al.  Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. , 1992, The EMBO journal.

[13]  A. Fersht,et al.  Cooperativity in ATP hydrolysis by GroEL is increased by GroES , 1991, FEBS letters.

[14]  V. Shubin,et al.  High molecular weight pea leaf protein similar to the groE protein of escherichia coli , 1982 .

[15]  H. Taguchi,et al.  Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody. , 1994, Journal of molecular biology.

[16]  G. Lorimer,et al.  Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. , 1993, Biochemistry.

[17]  F. Hartl,et al.  Molecular chaperone functions of heat-shock proteins. , 1993, Annual review of biochemistry.

[18]  R. Hallberg,et al.  A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophila , 1987, Molecular and cellular biology.

[19]  John O. Thomas,et al.  A cytoplasmic chaperonin that catalyzes β-actin folding , 1992, Cell.

[20]  M. Kessel,et al.  Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. , 1994, Science.

[21]  C Chothia,et al.  Surface, subunit interfaces and interior of oligomeric proteins. , 1988, Journal of molecular biology.

[22]  C. Georgopoulos,et al.  The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures , 1989, Journal of bacteriology.

[23]  G. Lorimer,et al.  Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP , 1989, Nature.

[24]  G. Lorimer,et al.  Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. , 1994, Science.

[25]  S. Chen,et al.  ATP induces large quaternary rearrangements in a cage-like chaperonin structure , 1993, Current Biology.

[26]  J. Buchner,et al.  On the role of groES in the chaperonin-assisted folding reaction. Three case studies. , 1994, The Journal of biological chemistry.

[27]  G. Lorimer,et al.  Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry. , 1991, The Journal of biological chemistry.

[28]  N. Lissin,et al.  The strongly conserved carboxyl‐terminus glycine‐methionine motif of the Escherichia coli GroEL chaperonin is dispensable , 1993, Molecular microbiology.

[29]  Yechezkel Kashi,et al.  GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms , 1994, Cell.

[30]  R. Hendrix.  Purification and properties of groE, a host protein involved in bacteriophage assembly. , 1979, Journal of molecular biology.

[31]  T. Langer,et al.  The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding , 1993, Nature.

[32]  F. Hartl,et al.  Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria , 1989, Nature.

[33]  G. Lorimer,et al.  Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring. , 1992, The Journal of biological chemistry.

[34]  F. Hartl,et al.  Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate , 1991, Nature.

[35]  P. Fitzgerald.  MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement , 1988 .

[36]  K. Kuwajima,et al.  The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state , 1994, Nature Structural Biology.

[37]  Y. Kashi,et al.  Residues in chaperonin GroEL required for polypeptide binding and release , 1994, Nature.

[38]  C. Chothia,et al.  The structure of protein-protein recognition sites. , 1990, The Journal of biological chemistry.

[39]  M. Culbertson,et al.  The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes , 1991, Molecular and cellular biology.

[40]  J. Rothman,et al.  Positive cooperativity in the functioning of molecular chaperone GroEL. , 1992, The Journal of biological chemistry.

[41]  T. Atkinson,et al.  Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. , 1993, Biochemistry.

[42]  B. Lee,et al.  The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.

[43]  N. Dixon,et al.  The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallography. , 1994, Journal of Molecular Biology.

[44]  K. Willison,et al.  Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. , 1993 .

[45]  J. Sambrook,et al.  Protein folding in the cell , 1992, Nature.

[46]  R. Jaenicke,et al.  Symmetric complexes of GroE chaperonins as part of the functional cycle. , 1994, Science.