1udv
Crystal structure of the hyperthermophilic archaeal dna-binding protein Sso10b2 at 1.85 A
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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 with ZN as ligand. 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
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