H. Baumann et al., SOLUTION STRUCTURE AND DNA-BINDING PROPERTIES OF A THERMOSTABLE PROTEIN FROM THE ARCHAEON SULFOLOBUS-SOLFATARICUS, Nature structural biology, 1(11), 1994, pp. 808-819
The archaeon Sulfolobus solfataricus expresses large amounts of a smal
l basic protein, Sso7d, which was previously identified as a DNA-bindi
ng protein possibly involved in compaction of DNA. We have determined
the solution structure of Sso7d. The protein consists of a triple-stra
nded anti-parallel beta-sheet onto which an orthogonal double-stranded
beta-sheet is packed. This topology is very similar to that found in
eukaryotic Src homology-3 (SH3) domains. Sso7d binds strongly (K-d < 1
0 mu M) to double-stranded DNA and protects it from thermal denaturati
on. in addition, we note that epsilon-mono-methylation of lysine side
chains of Sso7d is governed by cell growth temperatures, suggesting th
at methylation is related to the heat-shock response.