Abstract
The crystal structure of the DNA-binding domain of E. coli SSB (EcoSSB) has been determined to a resolution of 2.5 A. This is the first reported structure of a prokaryotic SSB. The structure of the DNA-binding domain of the E. coli protein is compared to that of the human mitochondrial SSB (HsmtSSB). In spite of the relatively low sequence identity between them, the two proteins display a high degree of structural similarity. EcoSSB crystallises with two dimers in the asymmetric unit, unlike HsmtSSB which contains only a dimer. This is probably a consequence: of the different polypeptide chain lengths in the EcoSSB heterotetramer. Crucial differences in the dimer-dimer interface of EcoSSB may account for the inability of EcoSSB and HsmtSSB to form cross-species heterotetramers, in contrast to many bacterial SSBs.
| Originalsprache | Englisch |
|---|---|
| Zeitschrift | FEBS Letters |
| Jahrgang | 411 |
| Ausgabenummer | 2-3 |
| Seiten (von - bis) | 313-316 |
| Seitenumfang | 4 |
| ISSN | 0014-5793 |
| DOIs | |
| Publikationsstatus | Veröffentlicht - 14.07.1997 |
Fördermittel
We thank F. Pasutto and J.R. Mesters for improving the EcoSSB crystallisation procedure and D. Geller, U. Gröbner, J. Hoven and L. Litz for technical support. The expert advice of A. Savoia and his coworkers during data collection at Sincrotrone Trieste is gratefully acknowledged. Work at Hannover was supported by the Deutsche Forschungsgemeinschaft.
Strategische Forschungsbereiche und Zentren
- Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)