|Proteins (2007) 66(2):266-71|
|Northeast Structural Genomics Consortium|
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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 PilZ domains are the long-sought c-di-GMP adaptor proteins.
|chemistry analogs & derivatives metabolism |
|Models, Molecular Protein Structure, Tertiary Adaptor Proteins, Signal Transducing Molecular Sequence Data Pseudomonas aeruginosa Protein Conformation Sequence Alignment Cyclic GMP Binding Sites Amino Acid Sequence Nuclear Magnetic Resonance, Biomolecular Protein Binding Sequence Homology, Amino Acid Bacterial Proteins Vibrio cholerae |
|52 (Last update: 04/21/2018 1:03:38pm)|
|Proteins. 2007 Feb 1;66(2):266-71.|