1udv: Difference between revisions
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'''Crystal structure of the hyperthermophilic archaeal dna-binding protein Sso10b2 at 1.85 A''' | '''Crystal structure of the hyperthermophilic archaeal dna-binding protein Sso10b2 at 1.85 A''' | ||
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[[Category: Lin, T W.]] | [[Category: Lin, T W.]] | ||
[[Category: Wang, A H.J.]] | [[Category: Wang, A H.J.]] | ||
[[Category: | [[Category: Dna binding protein]] | ||
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Revision as of 11:05, 3 May 2008
Crystal structure of the hyperthermophilic archaeal dna-binding protein Sso10b2 at 1.85 A
OverviewOverview
The crystal structure of a small, basic DNA binding protein, Sso10b2, from the thermoacidophilic archaeon Sulfolobus solfataricus was determined by the Zn multiwavelength anomalous diffraction method and refined to 1.85 A resolution. The 89-amino-acid protein adopts a betaalphabetaalphabetabeta topology. The structure is similar to that of Sso10b1 (also called Alba) from the same organism. However, Sso10b2 contains an arginine-rich loop RDRRR motif, which may play an important role in nucleic acid binding. There are two independent Sso10b2 proteins in the asymmetric unit, and a plausible stable dimer could be deduced from the crystal structure. Topology comparison revealed that Sso10b2 is similar to several RNA-binding proteins, including IF3-C, YhhP, and DNase I. Models of the Sso10b2 dimer bound to either B-DNA or A-DNA have been constructed.
About this StructureAbout this Structure
1UDV is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the hyperthermophilic archaeal DNA-binding protein Sso10b2 at a resolution of 1.85 Angstroms., Chou CC, Lin TW, Chen CY, Wang AH, J Bacteriol. 2003 Jul;185(14):4066-73. PMID:12837780 Page seeded by OCA on Sat May 3 11:05:00 2008