ArticleProtein science : a publication of the Protein Society2003
Crystal structure of a DNA binding protein from the hyperthermophilic euryarchaeon Methanococcus jannaschii.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 23 citations in OpenAlex.
- Dual dimeric interactions in the nucleic acid-binding protein Sac10b lead to multiple bridging of double-stranded DNA.Heliyon · 2024Article
- Identification of a Zika NS2B epitope as a biomarker for severe clinical phenotypes.RSC medicinal chemistry · 2021Article
- The Sac10b homolog from Sulfolobus islandicus is an RNA chaperone.Nucleic acids research · 2020Article
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- Biochemical and structural insights into RNA binding by Ssh10b, a member of the highly conserved Sac10b protein family in Archaea.The Journal of biological chemistry · 2014Article
- Crystal structure of archaeal chromatin protein Alba2-double-stranded DNA complex from Aeropyrum pernix K1.The Journal of biological chemistry · 2012Article
- Identification and molecular characterization of an Alba-family protein from human malaria parasite Plasmodium falciparum.Nucleic acids research · 2012Article
- Molecular mechanism underlying the interaction of typical Sac10b family proteins with DNA.PloS one · 2012Article
- Article
- Article
- Dimer-dimer stacking interactions are important for nucleic acid binding by the archaeal chromatin protein Alba.The Biochemical journal · 2010Article
- The Sac10b homolog in Methanococcus maripaludis binds DNA at specific sites.Journal of bacteriology · 2009Article
- Archaeal chromatin proteins histone HMtB and Alba have lost DNA-binding ability in laboratory strains of Methanothermobacter thermautotrophicus.Extremophiles : life under extreme conditions · 2008Article
- Posttranslational protein modification in Archaea.Microbiology and molecular biology reviews : MMBR · 2005Review
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8 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The Sac10b family consists of a group of highly conserved DNA binding proteins from both the euryarchaeotal and the crenarchaeotal branches of Archaea. The proteins have been suggested to play an architectural role in the chromosomal organization in these organisms. Previous studies have mainly focused on the Sac10b proteins from the crenarchaeota. Here, we report the 2.0 A resolution crystal structure of Mja10b from the euryarchaeon Methanococcus jannaschii. The model of Mja10b has been refined to an R-factor of 20.9%. The crystal structure of an Mja10b monomer reveals an alpha/beta structure of four beta-strands and two alpha-helices, and Mja10b assembles into a dimer via an extensive hydrophobic interface. Mja10b has a similar topology to that of its crenarchaeota counterpart Sso10b (also known as Alba). Structural comparison between the two proteins suggests that structural features such as hydrophobic inner core, acetylation sites, dimer interface, and DNA binding surface are conserved among Sac10b proteins. Structural differences between the two proteins were found in the loops. To understand the structural basis for the thermostability of Mja10b, the Mja10b structure was compared to other proteins with similar topology. Our data suggest that extensive ion-pair networks, optimized accessible surface area and the dimerization via hydrophobic interactions may contribute to the enhanced thermostability of Mja10b.
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