Unique active site formation in a novel galactose 1‐phosphate uridylyltransferase from the hyperthermophilic archaeon Pyrobaculum aerophilum

2020 ◽  
Vol 88 (5) ◽  
pp. 669-678 ◽  
Author(s):  
Tatsuya Ohshida ◽  
Junji Hayashi ◽  
Kazunari Yoneda ◽  
Toshihisa Ohshima ◽  
Haruhiko Sakuraba
2007 ◽  
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Christian Löw ◽  
Ulrich Weininger ◽  
Markus Zeeb ◽  
Wei Zhang ◽  
Ernest D. Laue ◽  
...  

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Anthony J. Choi ◽  
Jeffrey H. Miller ◽  
Karl O. Stetter ◽  
Melvin I. Simon ◽  
...  

1996 ◽  
Vol 24 (22) ◽  
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P. Markiewicz ◽  
C. Baikalov ◽  
S. Fitz-Gibbon ◽  
K. O. Stetter ◽  
...  

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M.K. Nahas ◽  
A.-C. Déclais ◽  
...  

Branched helical junctions are common in nucleic acids. In DNA, the four-way junction (Holliday junction) is an essential intermediate in homologous recombination and is a highly dynamic structure, capable of stacking conformer transitions and branch migration. Our single-molecule fluorescence studies provide unique insight into the energy landscape of Holliday junctions by visualizing these processes directly. In the hairpin ribozyme, an RNA four-way junction is an important structural element that enhances active-site formation by several orders of magnitude. Our single-molecule studies suggest a plausible mechanism for how the junction achieves this remarkable feat; the structural dynamics of the four-way junction bring about frequent contacts between the loops that are needed to form the active site. The most definitive evidence for this is the observation of three-state folding in single-hairpin ribozymes, the intermediate state of which is populated due to the intrinsic properties of the junction.


2010 ◽  
Vol 502 (2) ◽  
pp. 81-88 ◽  
Author(s):  
Haruhiko Sakuraba ◽  
Kaori Yokono ◽  
Kazunari Yoneda ◽  
Akira Watanabe ◽  
Yasuhiko Asada ◽  
...  

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