Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding - Test2 - elhamkhani - TriplyDB

Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding

Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding

http://www.wikidata.org/entity/Q27657699

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Structural basis for the allosteric control of the global transcription factor NtcA by the nitrogen starvation signal 2-oxoglutarate Structural basis for the regulation of NtcA-dependent transcription by proteins PipX and PII Crystal Structure of the Pseudomonas aeruginosa Virulence Factor Regulator Cyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosis The Structure of Bradyrhizobium japonicum Transcription Factor FixK2 Unveils Sites of DNA Binding and Oxidation X-ray crystal structure of TTHB099, a CRP/FNR superfamily transcriptional regulator from Thermus thermophilus HB8, reveals a DNA-binding protein with no required allosteric effector molecule Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers The crystal structures of apo and cAMP-bound GlxR from Corynebacterium glutamicum reveal structural and dynamic changes upon cAMP binding in CRP/FNR family transcription factors Crystallization and preliminary X-ray analysis of the ligand-binding domain of cAMP receptor protein.Improving acetate tolerance of Escherichia coli by rewiring its global regulator cAMP receptor protein (CRP).Resolution of mixed site DNA complexes with dimer-forming minor-groove binders by using electrospray ionization mass spectrometry: compound structure and DNA sequence effects.Gating of the MlotiK1 potassium channel involves large rearrangements of the cyclic nucleotide-binding domains.Effect of DNA binding on geminate CO recombination kinetics in CO-sensing transcription factor CooA.Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.The N-terminal capping propensities of the D-helix modulate the allosteric activation of the Escherichia coli cAMP receptor protein.DNA-binding properties of a cGMP-binding CRP homologue that controls development of metabolically dormant cysts of Rhodospirillum centenum.Crystallization and preliminary X-ray analysis of the CRP-cAMP-DNA (full length) complex Crystallization and preliminary X-ray diffraction analysis of D53H mutant Escherichia coli cAMP receptor protein.Cyclic-AMP and bacterial cyclic-AMP receptor proteins revisited: adaptation for different ecological niches Ligand responses of Vfr, the virulence factor regulator from Pseudomonas aeruginosa.Modulation of allosteric behavior through adjustment of the differential stability of the two interacting domains in E. coli cAMP receptor protein.cAMP receptor protein (CRP)-mediated resistance/tolerance in bacteria: mechanism and utilization in biotechnology.The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite.Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy.Asymmetric configurations in a reengineered homodimer reveal multiple subunit communication pathways in protein allostery.Using student-generated UV-induced Escherichia coli mutants in a directed inquiry undergraduate genetics laboratory.Aspartate 141 is the fourth ligand of the oxygen-sensing [4Fe-4S]2+ cluster of Bacillus subtilis transcriptional regulator Fnr.Structures during binding of cAMP receptor to promoter DNA: promoter search slowed by non-specific sites.Energetic redistribution in allostery to execute protein function.C-terminal dimerization of apo-cyclic AMP receptor protein validated in solution.Revisiting the mechanism of activation of cyclic AMP receptor protein (CRP) by cAMP in Escherichia coli: lessons from a subunit-crosslinked form of CRP.A genetic and physical study of the interdomain linker of E. Coli AraC protein--a trans-subunit communication pathway.SIMBAD: a sequence-independent molecular-replacement pipeline Theoretical analysis of inducer and operator binding for cyclic-AMP receptor protein mutants Dynamic binding

P2860

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P2860

Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding

http://www.wikidata.org/entity/Q27657699

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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Structure of apo-CAP reveals t ...... are necessary for DNA binding

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PNAS.0908380106

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Structure of apo-CAP reveals t ...... are necessary for DNA binding

@en

P2093

Hitesh Sharma

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Jilie Kong

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Jimin Wang

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Shaoning Yu

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Thomas A Steitz

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P2860

A short history of SHELX

Improved methods for building protein models in electron density maps and the location of errors in these models

Structure of the CO sensing transcription activator CooA

Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole

Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator

Structural basis for cAMP-mediated allosteric control of the catabolite activator protein.

The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer

Coot: model-building tools for molecular graphics

Likelihood-enhanced fast rotation functions

The CCP4 suite: programs for protein crystallography

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16604-16609

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scholarly article

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10.1073/PNAS.0908380106

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39

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106

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2009-09-16T00:00:00Z

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26871520

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19805344

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2745332

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