Analysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases
Author:
Affiliation:
1. Chemistry Department; M.V. Lomonosov Moscow State University; 1-3 Leninskiye Gory Moscow 119991 Russia
2. N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences; 4 Kosygin Street Moscow 119334 Russia
Funder
Russian Foundation for Basic Research
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.25108/fullpdf
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3. Structures of the catalytic EAL domain of the Escherichia coli direct oxygen sensor;Tarnawski;Acta Crystallogr D,2013
4. Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: a study of the EAL domain-containing RocR from Pseudomonas aeruginosa;Rao;J Bacteriol,2008
5. Structural insights into the regulatory mechanism of the response regulator RocR from Pseudomonas aeruginosa in cyclic di-GMP signaling;Chen;J Bacteriol,2012
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