Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-12

AUTHORS

K Braig, P D Adams, A T Brünger

ABSTRACT

Improved refinement of the crystal structure of GroEL from Escherichia coli has resulted in a complete atomic model for the first 524 residues. A new torsion-angle dynamics method and non-crystallographic symmetry restraints were used in the refinement. The model indicates that conformational variability exists due to rigid-body movements between the apical and intermediate domains of GroEL, resulting in deviations from strict seven-fold symmetry. The regions of the protein involved in polypeptide and GroES binding show unusually high B factors; these values may indicate mobility or discrete disorder. The variability of these regions may play a role in the ability of GroEL to bind a wide variety of substrates. More... »

PAGES

1083-1094

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb1295-1083

DOI

http://dx.doi.org/10.1038/nsb1295-1083

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1003523499

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8846220


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