NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein.

NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Research Abstract Details 

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NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Abstract Text:

Theresa A Ramelot,Adelinda Yee,John R Cort,Anthony Semesi,Cheryl H Arrowsmith,Michael A Kennedy,

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. Publishing Authors By Initials

TA Ramelot,A Yee,JR Cort,A Semesi,CH Arrowsmith,MA Kennedy,

For similar bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: vibrionaceae: vibrio: vibrio cholerae research abstracts see: bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: vibrionaceae: vibrio: vibrio cholerae research

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NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Proteins

VOLUME: 66

Page Numbers: 266-71

Journal Abbreviation: Proteins

ISSN: 1097-0134

DAY: 1

MONTH: Feb

YEAR: 2007

NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8700181

NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Keywords Mesh Terms:

KEYWORDS: Vibrio cholerae

MESH TERMS: chemistry

Chemical & Substance for Abstract: NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Information

Substance Name: Cyclic GMP

Registry Number: 7665-99-8

Grant and Affiliation Information for NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein.

AFFILIATION: Pacific Northwest National Laboratory, Biological Sciences Division, Richland, Washington 99354, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: P50-GM62413

ACRONYM: GM

MEDLINETA: Proteins

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