scholarly journals Rhomboids make do with a weak hydrogen bond

2019 ◽  
Vol 151 (3) ◽  
pp. 274-274 ◽  
Author(s):  
Caitlin Sedwick

JGP paper explores the strength of the hydrogen bond network at the active site of GlpG.

2014 ◽  
Vol 111 (52) ◽  
pp. 18454-18459 ◽  
Author(s):  
Lu Wang ◽  
Stephen D. Fried ◽  
Steven G. Boxer ◽  
Thomas E. Markland

2017 ◽  
Vol 121 (41) ◽  
pp. 7876-7881 ◽  
Author(s):  
Xiaolong Li ◽  
Yang Zheng ◽  
Junhua Chen ◽  
Jens-Uwe Grabow ◽  
Qian Gou ◽  
...  

Biochemistry ◽  
2007 ◽  
Vol 46 (27) ◽  
pp. 7973-7979 ◽  
Author(s):  
Harry A. Dailey ◽  
Chia-Kuei Wu ◽  
Peter Horanyi ◽  
Amy E. Medlock ◽  
Wided Najahi-Missaoui ◽  
...  

2016 ◽  
Vol 12 (10) ◽  
pp. 3139-3145 ◽  
Author(s):  
Fei Liao ◽  
Hong Yuan ◽  
Ke-Jie Du ◽  
Yong You ◽  
Shu-Qin Gao ◽  
...  

A single Tyr introduced in the secondary sphere of the heme active site in myoglobin at position 107 or 138 forms a distinct Tyr-associated H-bond network, regulating both the protein properties and functions.


1999 ◽  
Vol 274 (39) ◽  
pp. 27711-27716 ◽  
Author(s):  
Cecilia A. Ramilo ◽  
Vincent Leveque ◽  
Yue Guan ◽  
James R. Lepock ◽  
John A. Tainer ◽  
...  

Further examination of the active site region in our X-ray crystallographic model of subtilisin BPN' reveals a hydrogen-bond network that bears a remarkable resemblance to the one found in a- chymotrypsin. It involves the side chains of the reactive Ser-221, His-64, Asp-32 and Ser-33. Otherwise the two enzymes have entirely different three-dimensional structures. This observation suggests that the common hydrogen bond network plays some essential role in the catalytic mechanism of serine proteases generally.


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