DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ko, Junsang | ko |
dc.contributor.author | Ryu, Kyoung-Seok | ko |
dc.contributor.author | Kim, Henna | ko |
dc.contributor.author | Shin, Jae-Sun | ko |
dc.contributor.author | Lee, Jie-Oh | ko |
dc.contributor.author | Cheong, Chaejoon | ko |
dc.contributor.author | Choi, Byong-Seok | ko |
dc.date.accessioned | 2011-03-03T08:24:46Z | - |
dc.date.available | 2011-03-03T08:24:46Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2010-04 | - |
dc.identifier.citation | JOURNAL OF MOLECULAR BIOLOGY, v.398, no.1, pp.97 - 110 | - |
dc.identifier.issn | 0022-2836 | - |
dc.identifier.uri | http://hdl.handle.net/10203/22404 | - |
dc.description.abstract | Cyclic diguanylate (c-di-GMP) is a global regulator that modulates pathogen virulence and biofilm formation in bacteria. Although a bioinformatic study revealed that PilZ domain proteins are the long-sought c-di-GMP binding proteins, the mechanism by which c-di-GMP regulates them is uncertain. Pseudomonas putida PP4397 is one such protein that contains YcgR-N and PilZ domains and the apo-PP4397 structure was solved earlier by the Joint Center for Structural Genomics. We determined the crystal structure of holo-PP4397 and found that two intercalated c-di-GMPs fit into the junction of its YcgR-N and PilZ domains. Moreover, c-di-GMP binding induces PP4397 to undergo a dimer-to-monomer transition. Interestingly, another PilZ domain protein, VCA0042, binds to a single molecule of c-di-GMP, and both its apo and holo forms are dimeric. Mutational studies and the additional crystal structure of holo-VCA0042 (L135R) showed that the Arg122 residue of PP4397 is crucial for the recognition of two molecules of c-di-GMP. Thus, PilZ domain proteins exhibit different c-di-GMP binding stoichiometry and quaternary structure, and these differences are expected to play a role in generating diverse forms of c-di-GMP-mediated regulation. (C) 2010 Elsevier Ltd. All rights reserved. | - |
dc.description.sponsorship | This work was supported by the National Research Foundation of Korea (NRF; grants 2009-0092818 and 2009-220-C00036), and by the Bio-international cooperative research program from Chungcheongbuk-do Province. We thank Melissa Stauffer, PhD, of Scientific Editing Solutions, for editing the manuscript. | en |
dc.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | - |
dc.subject | CYCLIC DIGUANYLATE | - |
dc.subject | ALLOSTERIC CONTROL | - |
dc.subject | PSEUDOMONAS-AERUGINOSA | - |
dc.subject | SIGNAL-TRANSDUCTION | - |
dc.subject | BIOFILM FORMATION | - |
dc.subject | VIBRIO-CHOLERAE | - |
dc.subject | SYSTEM | - |
dc.subject | PHOSPHODIESTERASE | - |
dc.subject | CRYSTALLOGRAPHY | - |
dc.subject | IDENTIFICATION | - |
dc.title | Structure of PP4397 Reveals the Molecular Basis for Different c-di-GMP Binding Modes by Pilz Domain Proteins | - |
dc.type | Article | - |
dc.identifier.wosid | 000277219700008 | - |
dc.identifier.scopusid | 2-s2.0-77950859347 | - |
dc.type.rims | ART | - |
dc.citation.volume | 398 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 97 | - |
dc.citation.endingpage | 110 | - |
dc.citation.publicationname | JOURNAL OF MOLECULAR BIOLOGY | - |
dc.identifier.doi | 10.1016/j.jmb.2010.03.007 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Lee, Jie-Oh | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.contributor.nonIdAuthor | Ryu, Kyoung-Seok | - |
dc.contributor.nonIdAuthor | Cheong, Chaejoon | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | c-di-GMP | - |
dc.subject.keywordAuthor | PilZ domain protein | - |
dc.subject.keywordAuthor | PP4397 | - |
dc.subject.keywordAuthor | VCA0042 | - |
dc.subject.keywordPlus | CYCLIC DIGUANYLATE | - |
dc.subject.keywordPlus | ALLOSTERIC CONTROL | - |
dc.subject.keywordPlus | PSEUDOMONAS-AERUGINOSA | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | BIOFILM FORMATION | - |
dc.subject.keywordPlus | VIBRIO-CHOLERAE | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | PHOSPHODIESTERASE | - |
dc.subject.keywordPlus | CRYSTALLOGRAPHY | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
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