4PSN
Crystal structure of apeThermo-DBP-RP2
Summary for 4PSN
Entry DOI | 10.2210/pdb4psn/pdb |
Related | 4PSL 4PSM 4PSO |
Descriptor | ssDNA binding protein, IMIDAZOLE, GLYCEROL, ... (4 entities in total) |
Functional Keywords | ssdna binding protein, dna binding protein |
Biological source | Aeropyrum pernix |
Total number of polymer chains | 4 |
Total formula weight | 107671.10 |
Authors | Gahlei, H.,von Moeller, H.,Eppers, D.,Loll, B.,Wahl, M.C. (deposition date: 2014-03-07, release date: 2014-04-30, Last modification date: 2024-10-30) |
Primary citation | Ghalei, H.,Moeller, H.v.,Eppers, D.,Sohmen, D.,Wilson, D.N.,Loll, B.,Wahl, M.C. Entrapment of DNA in an intersubunit tunnel system of a single-stranded DNA-binding protein. Nucleic Acids Res., 42:6698-6708, 2014 Cited by PubMed Abstract: Instead of a classical single-stranded deoxyribonuleic acid (DNA)-binding protein (SSB), some hyperthermophilic crenarchaea harbor a non-canonical SSB termed ThermoDBP. Two related but poorly characterized groups of proteins, which share the ThermoDBP N-terminal DNA-binding domain, have a broader phylogenetic distribution and co-exist with ThermoDBPs and/or other SSBs. We have investigated the nucleic acid binding properties and crystal structures of representatives of these groups of ThermoDBP-related proteins (ThermoDBP-RPs) 1 and 2. ThermoDBP-RP 1 and 2 oligomerize by different mechanisms and only ThermoDBP-RP2 exhibits strong single-stranded DNA affinity in vitro. A crystal structure of ThermoDBP-RP2 in complex with DNA reveals how the NTD common to ThermoDBPs and ThermoDBP-RPs can contact the nucleic acid in a manner that allows a symmetric homotetrameric protein complex to bind single-stranded DNA molecules asymmetrically. While single-stranded DNA wraps around the surface or binds along channels of previously investigated SSBs, it traverses an internal, intersubunit tunnel system of a ThermoDBP-RP2 tetramer. Our results indicate that some archaea have acquired special SSBs for genome maintenance in particularly challenging environments. PubMed: 24744237DOI: 10.1093/nar/gku259 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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