Synthetic models of the active site of catechol oxidase: mechanistic studies

2006 ◽  
Vol 35 (9) ◽  
pp. 814 ◽  
Author(s):  
Iryna A. Koval ◽  
Patrick Gamez ◽  
Catherine Belle ◽  
Katalin Selmeczi ◽  
Jan Reedijk
ChemInform ◽  
2006 ◽  
Vol 37 (48) ◽  
Author(s):  
Iryna A. Koval ◽  
Patrick Gamez ◽  
Catherine Belle ◽  
Katalin Selmeczi ◽  
Jan Reedijk

1989 ◽  
Vol 36 (3-4) ◽  
pp. 327
Author(s):  
T.N. Sorrell ◽  
M.L. Garrity ◽  
J.R. Richards ◽  
V.A. Vankai
Keyword(s):  

Author(s):  
Katie Coates ◽  
Timothy R. Walsh ◽  
James Spencer ◽  
Philip Hinchliffe

MCR-2 confers resistance to colistin, a `last-line' antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 Å resolution crystal structure of the catalytic domain of MCR-2 was determined. Variable amino acids are located distant from both the di-zinc active site and the membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.


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