Structural highlights
Function
[CDGBP_PSEAE] Binds the second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second-messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein.,Ramelot TA, Yee A, Cort JR, Semesi A, Arrowsmith CH, Kennedy MA Proteins. 2007 Feb 1;66(2):266-71. PMID:17096419[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ramelot TA, Yee A, Cort JR, Semesi A, Arrowsmith CH, Kennedy MA. NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Proteins. 2007 Feb 1;66(2):266-71. PMID:17096419 doi:10.1002/prot.21199
- ↑ Shin JS, Ryu KS, Ko J, Lee A, Choi BS. Structural characterization reveals that a PilZ domain protein undergoes substantial conformational change upon binding to cyclic dimeric guanosine monophosphate. Protein Sci. 2011 Feb;20(2):270-7. doi: 10.1002/pro.557. Epub 2010 Dec 23. PMID:21280119 doi:http://dx.doi.org/10.1002/pro.557
- ↑ Habazettl J, Allan MG, Jenal U, Grzesiek S. Solution structure of the PilZ domain protein PA4608 complex with c-di-GMP identifies charge clustering as molecular readout. J Biol Chem. 2011 Feb 10. PMID:21310957 doi:10.1074/jbc.M110.209007
- ↑ Ramelot TA, Yee A, Cort JR, Semesi A, Arrowsmith CH, Kennedy MA. NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Proteins. 2007 Feb 1;66(2):266-71. PMID:17096419 doi:10.1002/prot.21199
