Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin

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.

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

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

2009 ◽  
Vol 48 (39) ◽  
pp. 7171-7175 ◽  
Author(s):  
Marcello Forconi ◽  
Raghuvir N. Sengupta ◽  
Mao-Chin Liu ◽  
Alan C. Sartorelli ◽  
Joseph A. Piccirilli ◽  
...  

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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