4HW0

Crystal structure of Sso10a-2, a DNA-binding protein from Sulfolobus solfataricus

Summary for 4HW0

• Entry DOI: 10.2210/pdb4hw0/pdb
• Descriptor: DNA-binding protein Sso10a-2 (2 entities in total)
• Functional Keywords: winged-helix, dna-binding domain, two-stranded antiparallel coiled-coil, dna/rna-binding 3-helical bundle, dna binding protein
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 3
• Total formula weight: 37109.90

Authors

Waterreus, W.J.,Goosen, N.,Moolenaar, G.F.,Driessen, R.P.C.,Dame, R.T.,Pannu, N.S. (deposition date: 2012-11-07, release date: 2013-10-30, Last modification date: 2024-11-20)

Primary citation

Driessen, R.P.,Lin, S.N.,Waterreus, W.J.,van der Meulen, A.L.,van der Valk, R.A.,Laurens, N.,Moolenaar, G.F.,Pannu, N.S.,Wuite, G.J.,Goosen, N.,Dame, R.T.
Diverse architectural properties of Sso10a proteins: Evidence for a role in chromatin compaction and organization.
Sci Rep, 6:29422-29422, 2016

PubMed Abstract: Sso10a proteins are small DNA-binding proteins expressed by the crenarchaeal model organism Sulfolobus solfataricus. Based on the structure of Sso10a1, which contains a winged helix-turn-helix motif, it is believed that Sso10a proteins function as sequence-specific transcription factors. Here we show that Sso10a1 and Sso10a2 exhibit different distinct DNA-binding modes. While the ability to bend DNA is shared between the two proteins, DNA bridging is observed only for Sso10a1 and only Sso10a2 exhibits filament formation along DNA. The architectural properties of Sso10a proteins suggest that these proteins fulfil generic roles in chromatin organization and compaction. As these proteins exhibit different binding behaviour depending on their DNA binding stoichiometry, altered levels of expression in the cell can be exploited to drive changes in local genome folding, which may operate to modulate transcription.

PubMed: 27403582
DOI: 10.1038/srep29422

Experimental method

X-RAY DIFFRACTION (2 Å)