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| CONFORMATIONAL VARIABILITY IN THE REFINED STRUCTURE OF THE CHAPERONIN GROEL AT 2.8 ANGSTROM RESOLUTION |
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| Author(s): BRAIG K, ADAMS PD, BRUNGER AT |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 2 Issue: 12 Pages: 1083-1094 Published: DEC 1995 |
| Times Cited: 161 References: 41 |
| 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. YALE UNIV, HOWARD HUGHES MED INST, NEW HAVEN, CT 06520 USA
2. YALE UNIV, DEPT GENET, NEW HAVEN, CT 06510 USA
3. YALE UNIV, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06520 USA |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: TH949 |
| ISSN: 1072-8368 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |