scholarly journals Crystal Structure of Cardiac Ryanodine Receptor N-Terminal Region Contains Unique Anion Binding Site Targeted by Disease-Associated Mutations

2014 ◽  
Vol 106 (2) ◽  
pp. 108a
Author(s):  
Lynn Kimlicka ◽  
Ching-Chieh Tung ◽  
Anna-Carin C. Carlsson ◽  
Paolo A. Lobo ◽  
Zhiguang Yuchi ◽  
...  
Structure ◽  
2013 ◽  
Vol 21 (8) ◽  
pp. 1440-1449 ◽  
Author(s):  
Lynn Kimlicka ◽  
Ching-Chieh Tung ◽  
Anna-Carin Cecilia Carlsson ◽  
Paolo Antonio Lobo ◽  
Zhiguang Yuchi ◽  
...  

2013 ◽  
Vol 20 (11) ◽  
pp. 1211-1216 ◽  
Author(s):  
L’ubomír Borko ◽  
Július Kostan ◽  
Alexandra Zahradníkova ◽  
Vladimír Pevala ◽  
Juraj Gasperík ◽  
...  

2021 ◽  
pp. 101412
Author(s):  
Jingyan Zhang ◽  
Daniel P. Singh ◽  
Christopher Y. Ko ◽  
Roman Nikolaienko ◽  
Siobhan M. Wong King Yuen ◽  
...  

2012 ◽  
Vol 83 (11) ◽  
pp. 1523-1529 ◽  
Author(s):  
Dan Liu ◽  
Ruwani Hewawasam ◽  
Yamuna Karunasekara ◽  
Marco G. Casarotto ◽  
Angela F. Dulhunty ◽  
...  

2015 ◽  
Vol 467 (1) ◽  
pp. 177-190 ◽  
Author(s):  
Tao Mi ◽  
Zhichao Xiao ◽  
Wenting Guo ◽  
Yijun Tang ◽  
Florian Hiess ◽  
...  

Cys3602 in cardiac ryanodine receptor (RyR) mediates the action of the thiol agent N-ethylmaleimide, but not 4,4′-dithiodipyridine (DTDP). A central region encompassing the calmodulin (CaM)-binding site and Cys3602 in cardiac RyR represents an important determinant of calcium-release activation and termination.


2005 ◽  
Vol 187 (9) ◽  
pp. 3201-3205 ◽  
Author(s):  
Bin Huang ◽  
Matthew W. Vetting ◽  
Steven L. Roderick

ABSTRACT The biosynthesis of cysteine in bacteria and plants is carried out by a two-step pathway, catalyzed by serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS; O-acetylserine [thiol] lyase). The aerobic form of OASS forms a tight bienzyme complex with SAT in vivo, termed cysteine synthase. We have determined the crystal structure of OASS in complex with a C-terminal peptide of SAT required for bienzyme complex formation. The binding site of the peptide is at the active site of OASS, and its C-terminal carboxyl group occupies the same anion binding pocket as the α-carboxylate of the O-acetylserine substrate of OASS. These results explain the partial inhibition of OASS by SAT on complex formation as well as the competitive dissociation of the complex by O-acetylserine.


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