1NH9

Crystal Structure of a DNA Binding Protein Mja10b from the hyperthermophile Methanococcus jannaschii

Summary for 1NH9

• Entry DOI: 10.2210/pdb1nh9/pdb
• Descriptor: DNA-binding protein Alba (2 entities in total)
• Functional Keywords: mja10b, dna binding protein
• Biological source: Methanocaldococcus jannaschii
• Cellular location: Cytoplasm (Probable): Q57665
• Total number of polymer chains: 1
• Total formula weight: 9690.52

Authors

Wang, G.,Bartlam, M.,Guo, R.,Yang, H.,Xue, H.,Liu, Y.,Huang, L.,Rao, Z. (deposition date: 2002-12-19, release date: 2003-12-23, Last modification date: 2023-10-25)

Primary citation

Wang, G.,Guo, R.,Bartlam, M.,Yang, H.,Xue, H.,Liu, Y.,Huang, L.,Rao, Z.
Crystal structure of a DNA binding protein from the hyperthermophilic euryarchaeon Methanococcus jannaschii
Protein Sci., 12:2815-2822, 2003

PubMed 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.

PubMed: 14627741
DOI: 10.1110/ps.03325103

Experimental method

X-RAY DIFFRACTION (2 Å)