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| The 2.4 angstrom crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S |
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| Author(s): Boisvert DC, Wang JM, Otwinowski Z, Horwich AL, Sigler PB |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 3 Issue: 2 Pages: 170-177 Published: FEB 1996 |
| Times Cited: 188 References: 48 |
| Abstract: GroEL is a bacterial chaperonin of 14 identical subunits required to help fold newly synthesized proteins. The crystal structure of GroEL with ATP gamma S bound to each subunit shows that ATP hinds to a novel pocket, whose primary sequence is highly conserved among chaperonins. Interaction of Mg2+ and ATP involves phosphate oxygens of the alpha-, beta- and gamma-phosphates, which is unique for known structures of nucleotide-binding proteins. Although bound ATP induces modest conformational shifts in the equatorial domain, the stereochemistry that functionally coordinates GroEL's affinity for nucleotides, polypeptide, and GroES remains uncertain. |
| Document Type: Article |
| Language: English |
Addresses:
1. YALE UNIV, SCH MED, BOYER CTR, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06510 USA
2. YALE UNIV, SCH MED, BOYER CTR, DEPT GENET, NEW HAVEN, CT 06510 USA
3. YALE UNIV, SCH MED, BOYER CTR, HOWARD HUGHES MED INST, NEW HAVEN, CT 06510 USA |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: TT674 |
| ISSN: 1072-8368 |
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