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| THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM |
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| Author(s): BRAIG K, OTWINOWSKI Z, HEGDE R, BOISVERT DC, JOACHIMIAK A, HORWICH AL, SIGLER PB |
| Source: NATURE Volume: 371 Issue: 6498 Pages: 578-586 Published: OCT 13 1994 |
| Times Cited: 876 References: 52 |
| Abstract: 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 targe 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 mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder. |
| Document Type: Article |
| Language: English |
Addresses:
1. YALE UNIV, SCH MED, BOYER CTR, HOWARD HUGHES MED INST, NEW HAVEN, CT 06510 USA
2. YALE UNIV, SCH MED, DEPT GENET, NEW HAVEN, CT 06510 USA
3. YALE UNIV, SCH MED, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06510 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: PL559 |
| ISSN: 0028-0836 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |