1YWU

Solution NMR structure of Pseudomonas Aeruginosa protein PA4608. Northeast Structural Genomics target PaT7

Summary for 1YWU

• Entry DOI: 10.2210/pdb1ywu/pdb
• Descriptor: hypothetical protein PA4608 (1 entity in total)
• Functional Keywords: pa4608, pat7, beta barrel, pilz domain, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 17307.25

Authors

Ramelot, T.A.,Yee, A.A.,Cort, J.R.,Semesi, A.,Arrowsmith, C.H.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2005-02-18, release date: 2005-03-29, Last modification date: 2024-05-01)

Primary citation

Ramelot, T.A.,Yee, A.,Cort, J.R.,Semesi, A.,Arrowsmith, C.H.,Kennedy, M.A.
NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein.
Proteins, 66:266-271, 2007

PubMed Abstract: 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.

PubMed: 17096419
DOI: 10.1002/prot.21199

Experimental method

SOLUTION NMR