Journal article
A common core for binding single-stranded DNA: structural comparison of the single-stranded DNA-binding proteins (SSB) from E. coli and human mitochondria
FEBS letters, Vol.411(2), pp.313-316
1997
Handle:
https://hdl.handle.net/2376/108655
PMID: 9271227
Abstract
The crystal structure of the DNA-binding domain of E. coli SSB ( EcoSSB) has been determined to a resolution of 2.5 Å. 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.
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Details
- Title
- A common core for binding single-stranded DNA: structural comparison of the single-stranded DNA-binding proteins (SSB) from E. coli and human mitochondria
- Creators
- Gordon Webster - Department of Structural Biology and Crystallography, Institute of Molecular Biotechnology, Beutenbergstrasse 11, D-07745 Jena, GermanyJochen Genschel - Department of Structural Biology and Crystallography, Institute of Molecular Biotechnology, Beutenbergstrasse 11, D-07745 Jena, GermanyUte Curth - Department of Structural Biology and Crystallography, Institute of Molecular Biotechnology, Beutenbergstrasse 11, D-07745 Jena, GermanyClaus Urbanke - Department of Structural Biology and Crystallography, Institute of Molecular Biotechnology, Beutenbergstrasse 11, D-07745 Jena, GermanyChulHee Kang - Department of Structural Biology and Crystallography, Institute of Molecular Biotechnology, Beutenbergstrasse 11, D-07745 Jena, GermanyRolf Hilgenfeld
- Publication Details
- FEBS letters, Vol.411(2), pp.313-316
- Academic Unit
- Department of Chemistry
- Publisher
- Elsevier B.V
- Number of pages
- 4
- Identifiers
- 99900546759101842
- Language
- English
- Resource Type
- Journal article