Structural highlights
Function
[SSB_HUMAN] This protein binds preferentially and cooperatively to ss-DNA. Probably involved in mitochondrial DNA replication. Associates with mitochondrial DNA.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We solved the crystal structure of the homotetrameric single-stranded DNA binding (SSB) protein from human mitochondria at a resolution of 2.4 A. The tetramer is formed by two dimers interacting head-to-head and shows D2 symmetry. Sequence-related tetrameric SSB proteins occur in prokaryotes and eukaryotic mitochondria; this is the first report of an atomic resolution structure of this type of protein. Using biochemical data and analysis of sequence homologies, we were able to correlate the functional properties with structure. We propose that ssDNA wraps around the tetrameric HsmtSSB protein through electropositive channels guided by flexible loops.
Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 A resolution.,Yang C, Curth U, Urbanke C, Kang C Nat Struct Biol. 1997 Feb;4(2):153-7. PMID:9033597[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang C, Curth U, Urbanke C, Kang C. Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 A resolution. Nat Struct Biol. 1997 Feb;4(2):153-7. PMID:9033597
