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4PSN

Crystal structure of apeThermo-DBP-RP2

Summary for 4PSN
Entry DOI10.2210/pdb4psn/pdb
Related4PSL 4PSM 4PSO
DescriptorssDNA binding protein, IMIDAZOLE, GLYCEROL, ... (4 entities in total)
Functional Keywordsssdna binding protein, dna binding protein
Biological sourceAeropyrum pernix
Total number of polymer chains4
Total formula weight107671.10
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 citationGhalei, 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: 24744237
DOI: 10.1093/nar/gku259
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

237735

数据于2025-06-18公开中

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