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]
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
