Using Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling Complex - Test2 - elhamkhani - TriplyDB

Using Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling Complex

Using Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling Complex

http://www.wikidata.org/entity/Q27659885

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Prokaryotic 2-component systems and the OmpR/PhoB superfamily A Dual Binding Mode for RhoGTPases in Plexin Signalling The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima Solution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheY Branched Signal Wiring of an Essential Bacterial Cell-Cycle Phosphotransfer Protein Structural Basis of a Rationally Rewired Protein-Protein Interface Critical to Bacterial Signaling Conformational barrier of CheY3 and inability of CheY4 to bind FliM control the flagellar motor action in Vibrio cholerae Influence of the AgrC-AgrA Complex on the Response Time of Staphylococcus aureus Quorum Sensing Split histidine kinases enable ultrasensitivity and bistability in two-component signaling networks A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Functional characterization of type-B response regulators in the Arabidopsis cytokinin response.Modeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase.Systematic dissection and trajectory-scanning mutagenesis of the molecular interface that ensures specificity of two-component signaling pathways.Evolution of two-component signal transduction systems A specificity determinant for phosphorylation in a response regulator prevents in vivo cross-talk and modification by acetyl phosphate.A Social Medium: ASM's 5th Cell-Cell Communication in Bacteria Meeting in Review Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing.Mutational analysis of the P1 phosphorylation domain in Escherichia coli CheA, the signaling kinase for chemotaxis.Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action.Spatial organization in bacterial chemotaxis.The functional importance of co-evolving residues in proteins.Cross-talk and specificity in two-component signal transduction pathways.Spatial tethering of kinases to their substrates relaxes evolutionary constraints on specificity.Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp Chemosensory System: DIFFERENTIAL FUNCTION OF THE EIGHT PHOSPHOTRANSFERASE AND THREE RECEIVER DOMAINS.Comparative analysis of wolbachia genomes reveals streamlining and divergence of minimalist two-component systems.Destabilization of interaction between cytokinin signaling intermediates AHP1 and ARR4 modulates Arabidopsis development.Two Proteins Form a Heteromeric Bacterial Self-Recognition Complex in Which Variable Subdomains Determine Allele-Restricted Binding Adaptive mutations that prevent crosstalk enable the expansion of paralogous signaling protein families Evolving a robust signal transduction pathway from weak cross-talk.Genome sequence of Rhodobacter sphaeroides Strain WS8N.Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.Building interacting partner predictors using co-varying residue pairs between histidine kinase and response regulator pairs of 48 bacterial two-component systems.Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.

P2860

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P2860

Using Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling Complex

http://www.wikidata.org/entity/Q27659885

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

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2010年论文

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name

Using Structural Information t ...... Chemotaxis Signalling Complex

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Using Structural Information t ...... Chemotaxis Signalling Complex

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Using Structural Information t ...... Chemotaxis Signalling Complex

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Using Structural Information t ...... Chemotaxis Signalling Complex

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Using Structural Information t ...... Chemotaxis Signalling Complex

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Using Structural Information t ...... Chemotaxis Signalling Complex

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Using Structural Information t ...... Chemotaxis Signalling Complex

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Annabel Strawson

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Christian H Bell

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Judith P Armitage

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P2860

Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis

Electrostatics of nanosystems: application to microtubules and the ribosome

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction

Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxis

The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems

Crystal Structure of a Complex between the Phosphorelay Protein YPD1 and the Response Regulator Domain of SLN1 Bound to a Phosphoryl Analog

Crystal structure of Escherichia coli CheY refined at 1.7-A resolution

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e1000306

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10.1371/JOURNAL.PBIO.1000306

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2

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20161720

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2817712

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