Structural Basis for c-di-GMP-Mediated Inside-Out Signaling Controlling Periplasmic Proteolysis - sprookjes - yvandenbroek - TriplyDB

Structural Basis for c-di-GMP-Mediated Inside-Out Signaling Controlling Periplasmic Proteolysis

Structural Basis for c-di-GMP-Mediated Inside-Out Signaling Controlling Periplasmic Proteolysis

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Cyclic di-GMP: the first 25 years of a universal bacterial second messenger Microbiology, genomics, and clinical significance of the Pseudomonas fluorescens species complex, an unappreciated colonizer of humans Investigating the allosteric regulation of YfiN from Pseudomonas aeruginosa: clues from the structure of the catalytic domain Structural insights into the regulatory mechanism of the response regulator RocR from Pseudomonas aeruginosa in cyclic Di-GMP signaling.Structures of the PelD Cyclic Diguanylate Effector Involved in Pellicle Formation in Pseudomonas aeruginosa PAO1 Structural insight of a concentration-dependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motility Structure of the Cytoplasmic Region of PelD, a Degenerate Diguanylate Cyclase Receptor That Regulates Exopolysaccharide Production in Pseudomonas aeruginosa Structural Characterization of a Conserved, Calcium-Dependent Periplasmic Protease from Legionella pneumophila Inherent Regulation of EAL Domain-catalyzed Hydrolysis of Second Messenger Cyclic di-GMP Structures of the catalytic EAL domain of the Escherichia coli direct oxygen sensor Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: analysis of the reaction mechanism and novel roles for pGpG Structural and Biochemical Analysis of Tyrosine Phosphatase Related to Biofilm Formation A (TpbA) from the Opportunistic Pathogen Pseudomonas aeruginosa PAO1 Coincidence detection and bi-directional transmembrane signaling control a bacterial second messenger receptor.A c-di-GMP effector system controls cell adhesion by inside-out signaling and surface protein cleavage.Structural features of the Pseudomonas fluorescens biofilm adhesin LapA required for LapG-dependent cleavage, biofilm formation, and cell surface localization Cellular levels and binding of c-di-GMP control subcellular localization and activity of the Vibrio cholerae transcriptional regulator VpsT.Cell cycle constraints on capsulation and bacteriophage susceptibility Identification of flgZ as a flagellar gene encoding a PilZ domain protein that regulates swimming motility and biofilm formation in Pseudomonas Responses to elevated c-di-GMP levels in mutualistic and pathogenic plant-interacting bacteria Mechanistic insight into the conserved allosteric regulation of periplasmic proteolysis by the signaling molecule cyclic-di-GMP Systematic analysis of diguanylate cyclases that promote biofilm formation by Pseudomonas fluorescens Pf0-1.Differential analogue binding by two classes of c-di-GMP riboswitches Global Regulator MorA Affects Virulence-Associated Protease Secretion in Pseudomonas aeruginosa PAO1 Diguanylate cyclase null mutant reveals that C-Di-GMP pathway regulates the motility and adherence of the extremophile bacterium Acidithiobacillus caldus Dimeric c-di-GMP is required for post-translational regulation of alginate production in Pseudomonas aeruginosa.Sticky situations: key components that control bacterial surface attachment In situ proteolysis of the Vibrio cholerae matrix protein RbmA promotes biofilm recruitment.Homologs of the LapD-LapG c-di-GMP Effector System Control Biofilm Formation by Bordetella bronchiseptica.Crystallization studies of the murine c-di-GMP sensor protein STING.Sustained sensing as an emerging principle in second messenger signaling systems.LapG, required for modulating biofilm formation by Pseudomonas fluorescens Pf0-1, is a calcium-dependent protease Enzymatically active and inactive phosphodiesterases and diguanylate cyclases are involved in regulation of Motility or sessility in Escherichia coli CFT073 Contribution of Physical Interactions to Signaling Specificity between a Diguanylate Cyclase and Its Effector Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms.Crystallization and preliminary X-ray diffraction studies of Xanthomonas campestris PNPase in the presence of c-di-GMP.A systematic analysis of the role of GGDEF-EAL domain proteins in virulence and motility in Xanthomonas oryzae pv. oryzicola Structural insights into the regulatory mechanism of the Pseudomonas aeruginosa YfiBNR system.Single-cell and single-molecule analysis deciphers the localization, adhesion, and mechanics of the biofilm adhesin LapA.

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Structural Basis for c-di-GMP-Mediated Inside-Out Signaling Controlling Periplasmic Proteolysis

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2011 nî lūn-bûn

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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2011年の論文

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Structural Basis for c-di-GMP- ...... olling Periplasmic Proteolysis

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Structural Basis for c-di-GMP- ...... olling Periplasmic Proteolysis

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Dean R Madden

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Debashree Chatterjee

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George A O'Toole

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Marcos V A S Navarro

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Peter D Newell

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Petya V Krasteva

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Structural basis of activity and allosteric control of diguanylate cyclase

The structural basis of cyclic diguanylate signal transduction by PilZ domains

The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular PAS domain

Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition

A ligand-induced switch in the periplasmic domain of sensor histidine kinase CitA

Crystal Structure of a Functional Dimer of the PhoQ Sensor Domain

Phosphorylation-Independent Regulation of the Diguanylate Cyclase WspR

Crystal Structures of YkuI and Its Complex with Second Messenger Cyclic Di-GMP Suggest Catalytic Mechanism of Phosphodiester Bond Cleavage by EAL Domains

Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase

PILZ protein structure and interactions with PILB and the FIMX EAL domain: implications for control of type IV pilus biogenesis

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Holger Sondermann

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