Abstract
A complex between the headpiece amino-terminal residues 1 - 56 of lac repressor (HP56) and an 11-bp lac operator fragment was studied by H-1 NMR. The sequence specific assignment of the exchangeable and nonexchangeable protons has been accomplished. Several protons have favourable chemical shifts in the complex, therefore new intraprotein NOEs could be found that had not been unambigously identified in the free protein. By comparison, most of these intraprotein NOEs are also present in the spectra of the free headpiece but some are different. Furthermore, several new protein DNA NOEs could be identified. The NOE between the side-chain amide protons of Gln18 and C5H of C7 confirms the specific contact between these residues which was proposed from genetic experiments [Ebright, R.M. (1985) J. Biomol. Struct. & Dyn. 3,281 - 297]. The implications of the new data for the interaction between the lac repressor headpiece and its operator are discussed.
Original language | English |
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Pages (from-to) | 629-637 |
Number of pages | 9 |
Journal | European Journal of Biochemistry |
Volume | 194 |
Issue number | 2 |
Publication status | Published - 12 Dec 1990 |
Keywords
- NUCLEAR MAGNETIC-RESONANCE
- BINDING DOMAIN
- TRP REPRESSOR
- RESOLUTION
- RECOGNITION
- FRAGMENT
- PROTON
- LAMBDA
- MOTIF
- CRO