Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 66, Issue 2, Pages 266-271Publisher
WILEY
DOI: 10.1002/prot.21199
Keywords
NMR; PilZ; PA4608; c-di-GMP; second messenger; northeast structural genomics consortium; structural genomics; quorum sensing; Pseudomonas aeruginosa; biofilm formation
Categories
Funding
- NIGMS NIH HHS [P50-GM62413] Funding Source: Medline
Ask authors/readers for more resources
PA4608 is a 125 residue protein from Pseudomonas aeruginosa with a recent identification as a PilZ domain and putative bis-(3'-5')cyclic dimeric guanosine monophosphate (c-di-GMP) adaptor protein that plays a role in bacterial second-messenger regulated processes. The nuclear magnetic resonance (NMR) structure of PA4608 has been determined and c-di-GMP binding has been confirmed by NMR titration studies. The monomeric core structure of PA4608 contains a six-stranded anti-parallel beta barrel flanked by three helices. Conserved surface residues among PA4608 homologs suggest the c-di-GMP binding site is at one end of the barrel and includes residues in the helices as well as in the unstructured N-terminus. Chemical shift changes in PA4608 resonances upon titration with c-di-GMP confirm binding. This evidence supports the hypothesis that proteins containing PiIZ domains are the long-sought c-di-GMP adaptor proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available