Dcsbis (PA2771) from Pseudomonas aeruginosa is a highly active diguanylate cyclase with unique activity regulation

• DOI: 10.1038/srep29499
• Publication Date: 2016-07-08T09:03:51Z
• Authors: Ying Chen; Shiheng Liu; Cuilan Liu; Yan Huang; Kaikai Chi; Tiantian Su; Deyu Zhu; Jin Peng; Zhijie Xia; Jing He; Sujuan Xu; Wei Hu; Lichuan Gu
• Keywords: Second messenger system

Abstract C-di-GMP (3’,5’ -Cyclic diguanylic acid) is an important second messenger in bacteria that influences virulence, motility, biofilm formation, and cell division. The level of c-di-GMP cells controlled by diguanyl cyclases (DGCs) phosphodiesterases (PDEs). Here, we report the biochemical functions crystal structure potential diguanylase Dcsbis (PA2771, a diguanylate cyclase with self-blocked I-site) from Pseudomonas aeruginosa PAO1. full-length protein contains N-terminal GAF domain C-terminal GGDEF domain. We showed tightly coordinates motility without markedly affecting formation catalytic activity much higher than those many other DGCs. Unexpectedly, found peptide loop (protecting loop) extending occupies conserved inhibition site, thereby largely relieving product-inhibition effect. A large hydrophobic pocket was observed domain, thus suggesting unknown upstream signaling molecule may bind to moving protecting I-site turning off enzymatic activity.