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| Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae |
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| Author(s): Mande SC, Mehra V, Bloom BR, Hol WGJ |
| Source: SCIENCE Volume: 271 Issue: 5246 Pages: 203-207 Published: JAN 12 1996 |
| Times Cited: 104 References: 40 |
| Abstract: Members of the chaperonin-10 (cpn10) protein family, also called heat shock protein 10 and in Escherichia coli GroES, play an important role in ensuring the proper folding of many proteins. The crystal structure of the Mycobacterium leprae cpn10 (MI-cpn10) oligomer has been elucidated at a resolution of 3.5 angstroms. The architecture of the MI-cpn10 heptamer resembles a dome with an oculus in its roof. The inner surface of the dome is hydrophilic and highly charged. A flexible region, known to interact with cpn60, extends from the lower rim of the dome. With the structure of a cpn10 heptamer now revealed and the structure of the E. coli GroEL previously known, models of cpn10:cpn60 and GroEL:GroES complexes are proposed. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV WASHINGTON, DEPT BIOL STRUCT, SEATTLE, WA 98195 USA
2. UNIV WASHINGTON, BIOMOLEC STRUCT CTR, SEATTLE, WA 98195 USA
3. UNIV WASHINGTON, HOWARD HUGHES MED INST, SEATTLE, WA 98195 USA
4. UNIV WASHINGTON, DEPT MICROBIOL & IMMUNOL, SEATTLE, WA 98195 USA
5. ALBERT EINSTEIN COLL MED, HOWARD HUGHES MED INST, BRONX, NY 10461 USA |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: TP364 |
| ISSN: 0036-8075 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |