Article
Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre.
Molecular microbiology - 1 Jan 2014
Bellini Dom, Caly Delphine L, McCarthy Yvonne, Bumann Mario, An Shi-Qi, Dow J Maxwell, Ryan Robert P, Walsh Martin A
Abstract excerpt
Bis-(3',5') cyclic di-guanylate (c-di-GMP) is a key bacterial second messenger that is implicated in the regulation of many crucial processes that include biofilm formation, motility and virulence. Cellular levels of c-di-GMP are controlled through synthesis by GGDEF domain diguanylate cyclases and degradation by two classes of phosphodiesterase with EAL or HD-GYP domains. Here, we have determined the structure...
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