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 PubMedPA4608 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 AlsoReferences
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