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| CRYSTAL-STRUCTURE OF AN N-TERMINAL FRAGMENT OF THE DNA GYRASE B-PROTEIN |
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| Author(s): WIGLEY DB, DAVIES GJ, DODSON EJ, MAXWELL A, DODSON G |
| Source: NATURE Volume: 351 Issue: 6328 Pages: 624-629 Published: JUN 20 1991 |
| Times Cited: 369 References: 26 |
| Abstract: The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, complexed with a nonhydrolysable ATP analogue, has been solved at 2.5 angstrom resolution. It consists of two domains, both containing novel protein folds. The protein fragment forms a dimer, whose N-terminal domains are responsible for ATP binding and hydrolysis. The C-terminal domains form the sides of a 20 angstrom hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction. |
| Document Type: Article |
| Language: English |
| Reprint Address: WIGLEY, DB (reprint author), YORK UNIV, DEPT CHEM, YORK YO1 5DD, ENGLAND |
Addresses:
1. UNIV LEICESTER, DEPT BIOCHEM, LEICESTER LE1 7RH, ENGLAND |
| Publisher: MACMILLAN MAGAZINES LTD, 4 LITTLE ESSEX STREET, LONDON, ENGLAND WC2R 3LF |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: FT112 |
| ISSN: 0028-0836 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |