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7DWR

Structure of Sulfolobus solfataricus SegA-ADP complex bound to DNA

Summary for 7DWR
Entry DOI10.2210/pdb7dwr/pdb
DescriptorSOJ protein (Soj), DNA (5'-D(P*AP*GP*GP*GP*TP*GP*TP*TP*CP*CP*AP*CP*GP*TP*GP*AP*AP*AP*CP*AP*GP*GP*GP*A)-3'), DNA (5'-D(P*TP*CP*CP*CP*TP*GP*TP*TP*TP*CP*AP*CP*GP*TP*GP*GP*AP*AP*CP*AP*CP*CP*CP*T)-3'), ... (6 entities in total)
Functional Keywordspartition protein, dna binding protein-dna complex, dna binding protein
Biological sourceSaccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
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Total number of polymer chains8
Total formula weight128584.46
Authors
Yen, C.Y.,Lin, M.G.,Hsiao, C.D.,Sun, Y.J. (deposition date: 2021-01-17, release date: 2021-12-22, Last modification date: 2023-11-29)
Primary citationYen, C.Y.,Lin, M.G.,Chen, B.W.,Ng, I.W.,Read, N.,Kabli, A.F.,Wu, C.T.,Shen, Y.Y.,Chen, C.H.,Barilla, D.,Sun, Y.J.,Hsiao, C.D.
Chromosome segregation in Archaea: SegA- and SegB-DNA complex structures provide insights into segrosome assembly.
Nucleic Acids Res., 49:13150-13164, 2021
Cited by
PubMed Abstract: Genome segregation is a vital process in all organisms. Chromosome partitioning remains obscure in Archaea, the third domain of life. Here, we investigated the SegAB system from Sulfolobus solfataricus. SegA is a ParA Walker-type ATPase and SegB is a site-specific DNA-binding protein. We determined the structures of both proteins and those of SegA-DNA and SegB-DNA complexes. The SegA structure revealed an atypical, novel non-sandwich dimer that binds DNA either in the presence or in the absence of ATP. The SegB structure disclosed a ribbon-helix-helix motif through which the protein binds DNA site specifically. The association of multiple interacting SegB dimers with the DNA results in a higher order chromatin-like structure. The unstructured SegB N-terminus plays an essential catalytic role in stimulating SegA ATPase activity and an architectural regulatory role in segrosome (SegA-SegB-DNA) formation. Electron microscopy results also provide a compact ring-like segrosome structure related to chromosome organization. These findings contribute a novel mechanistic perspective on archaeal chromosome segregation.
PubMed: 34850144
DOI: 10.1093/nar/gkab1155
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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