| STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA |
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| Author(s): ABRAHAMS JP, LESLIE AGW, LUTTER R, WALKER JE |
| Source: NATURE Volume: 370 Issue: 6491 Pages: 621-628 Published: AUG 25 1994 |
| Times Cited: 1,851 References: 50 |
| Abstract: In the crystal structure of bovine mitochondrial F-1-ATPase determined at 2.8 Angstrom resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha(3) beta(3) subassembly relative to an alpha-helical domain of the gamma-subunit. |
| Document Type: Article |
| Language: English |
Addresses:
1. MRC, MOLEC BIOL LAB, CAMBRIDGE CB2 2QH, ENGLAND |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: PD310 |
| ISSN: 0028-0836 |