A common core for binding single-stranded DNA: structural comparison of the single-stranded DNA-binding proteins (SSB) from E. coli and human mitochondria.
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.
Webster
G
G
Department of Structural Biology and Crystallography, Institute of Molecular Biotechnology, Jena, Germany. gwebster@imb-jena.de
Genschel
J
J
Curth
U
U
Urbanke
C
C
Kang
C
C
Hilgenfeld
R
R
D018360:Crystallography, X-Ray; D004277:DNA, Single-Stranded / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry*; D006801:Humans; D008928:Mitochondria / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation
D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins