The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

Braig, Kerstin; Otwinowski, Zbyszek; Hegde, Rashmi S.; Boisvert, D.C.; Joachimiak, Andrzej; Horwich, Arthur L.; Sigler, Paul B.

doi:10.1038/371578a0

Cited by 1,316 publications

(1,259 citation statements)

References 46 publications

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“…Based on this structure, it is tempting to speculate that the side of GroES with a central protrusion would be the side that binds to GroEL and the protrusion could fit into the opening of the GroEL channel, because the diameter of the GroEL channel is also about 4.5 nm [23]. However, preliminary experiments seem to suggest otherwise.…”

Section: Resultsmentioning

confidence: 96%

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High resolution surface structure of E. coli GroES oligomer by atomic force microscopy

et al. 1996

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Using atomic force microscopy (AFM) in aqueous solution, we show that the surface structure of the oligomeric GroES can be obtained up to 10 A resolution. The seven subunits of the heptamer were well resolved without image averaging. The overall dimension of the GroES heptamer was 8.4+0.4 nm in diameter and 3.0+0.3 nm high. However, the AFM images further suggest that there is a central protrusion of 0.8+0.2 nm high and 4.5+0.4 nm in diameter on one side of GroES which displays a profound seven-fold symmetry. It was found that GroEL could not bind to the adsorbed GroES in the presence of AMP-PNP and Mg 2+, suggesting that the side of GroES with the central protrusion faces away from the GroEL lumen, because only one side of GroES was observed under these conditions. Based on the results from both electron and atomic force microscopy, a surface model for the GroES is proposed.Key words: Atomic force microscopy; GroES; GroEL; Resolution subunits were not discernible [18]. Because of the variable conformations observed by EM, it was even suggested that GroES could have a flexible structure or a symmetry other than the seven-fold [18]. Since the atomic force microscopy (AFM) has been shown to be capable of obtaining high resolution surface structures of several oligomeric bacterial proteins (for recent reviews, see [24][25][26]), we have applied this method to determine the surface structure of GroES under aqueous solutions. We show that the subunit structure can be clearly resolved in the AFM images without image processing/averaging. Surface structures beyond the subunits were also resolved, demonstrating a surface resolution of 10 A or so, which is much higher than that from EM images. In combination with the results from EM, a model for the GroES is also proposed. Materials and methods

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Section: Resultsmentioning

confidence: 96%

“…Although the structure of the GroEL tetradecamer has been solved to 2.8 ,4, resolution [23], the structure of GroES has only been elucidated by EM with negatively stained specimens [2,18]. Even with two-dimensional crystals, the GroES heptamer was only resolved as a ring of 7-8 nm, and the individual *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

High resolution surface structure of E. coli GroES oligomer by atomic force microscopy

et al. 1996

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“…Structurally, GroEL consists of two heptameric rings of identical subunits of 57 kDa each, stacked back-to-back (Braig et al, 1994). GroES, on the other hand, is a dome-shaped homoheptameric ring of 10 kDa subunits each that binds to the ends of the GroEL cylinder in the presence of ATP (Hunt et al, 1996) (Figure 6a).…”

Section: Ii4113 the Chaperoninsmentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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“…GroEL functions as a tetradecamer of two heptameric rings that stack back to back with a hydrophobic central cavity where substrate polypeptides are folded through alternate binding of the substrate and the co-chaperonin GroES (Braig et al 1994). Each subunit of GroEL is comprised of three domains, viz., the equatorial, the intermediate, and the apical domains.…”

Section: Introductionmentioning

confidence: 99%

Multiple Gene Duplication and Rapid Evolution in the groEL Gene: Functional Implications

2006

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Abstract. The chaperonins, GroEL and GroES, are present ubiquitously and provide a paradigm in the understanding of assisted protein folding. Due to its essentiality of function, GroEL exhibits high sequence conservation across species. Complete genome sequencing has shown the occurrence of duplicate or multiple copies of groEL genes in bacteria such as Mycobacterium tuberculosis and Corynebacterium glutamicum. Monophyly of each bacterial clade in the phylogenetic tree generated for the GroEL protein suggests a lineage-specific duplication. The duplicated groEL gene in Actinobacteria is not accompanied by the operonic groES despite the presence of upstream regulatory elements. Our analysis suggests that in these bacteria the duplicated groEL genes have undergone rapid evolution and divergence to function in a GroES-independent manner. Evaluation of multiple sequence alignment demonstrates that the duplicated genes have acquired mutations at functionally significant positions including those involved in substrate binding, ATP binding, and GroES binding and those involved in inter-ring and intra-ring interactions. We propose that the duplicate groEL genes in different bacterial clades have evolved independently to meet specific requirements of each clade. We also propose that the groEL gene, although essential and conserved, accumulates nonconservative substitutions to exhibit structural and functional variations.

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The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

Cited by 1,316 publications

References 46 publications

High resolution surface structure of E. coli GroES oligomer by atomic force microscopy

High resolution surface structure of E. coli GroES oligomer by atomic force microscopy

Firefly luciferase mutants as sensors of proteome stress

Multiple Gene Duplication and Rapid Evolution in the groEL Gene: Functional Implications

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