scholarly journals Crystal structure of a DNA binding protein from the hyperthermophilic euryarchaeonMethanococcus jannaschii

2003 ◽  
Vol 12 (12) ◽  
pp. 2815-2822 ◽  
Author(s):  
Ganggang Wang ◽  
Rong Guo ◽  
Mark Bartlam ◽  
Haitao Yang ◽  
Hong Xue ◽  
...  
2011 ◽  
Vol 286 (49) ◽  
pp. 42099-42104 ◽  
Author(s):  
Amit Sharma ◽  
Katherine R. Jenkins ◽  
Annie Héroux ◽  
Gregory D. Bowman

2019 ◽  
Vol 488 ◽  
pp. 182-194 ◽  
Author(s):  
Maryam Sedighipoor ◽  
Ali Hossein Kianfar ◽  
Gholamhossein Mohammadnezhad ◽  
Helmar Görls ◽  
Winfried Plass ◽  
...  

1997 ◽  
Vol 4 (2) ◽  
pp. 153-157 ◽  
Author(s):  
Cheng Yang ◽  
Ute Curth ◽  
Claus Urbanke ◽  
ChulHee Kang

2019 ◽  
Vol 47 (4) ◽  
pp. 1950-1963 ◽  
Author(s):  
Brian J Caldwell ◽  
Ekaterina Zakharova ◽  
Gabriel T Filsinger ◽  
Timothy M Wannier ◽  
Jordan P Hempfling ◽  
...  

2003 ◽  
Vol 185 (14) ◽  
pp. 4066-4073 ◽  
Author(s):  
Chia-Cheng Chou ◽  
Ting-Wan Lin ◽  
Chin-Yu Chen ◽  
Andrew H.-J. Wang

ABSTRACT 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 Å resolution. The 89-amino-acid protein adopts a βαβαββ 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.


Nature ◽  
1995 ◽  
Vol 376 (6538) ◽  
pp. 362-366 ◽  
Author(s):  
Yousif Shamoo ◽  
Alan M. Friedman ◽  
Mark R. Parsons ◽  
William H. Konigsberg ◽  
Thomas A. Steitz

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