Structural Insights into the Mechanism of the Allosteric Transitions of Mycobacterium tuberculosis cAMP Receptor Protein

Structural Insights into the Mechanism of the Allosteric Transitions of Mycobacterium tuberculosis cAMP Receptor Protein

Item
http://www.wikidata.org/entity/Q27657374
Modulation of Global Low-Frequency Motions Underlies Allosteric Regulation: Demonstration in CRP/FNR Family Transcription FactorsStructures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengersMycobacterium tuberculosis cAMP receptor protein (Rv3676) differs from the Escherichia coli paradigm in its cAMP binding and DNA binding properties and transcription activation propertiesReversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMPThe crystal structures of apo and cAMP-bound GlxR from Corynebacterium glutamicum reveal structural and dynamic changes upon cAMP binding in CRP/FNR family transcription factorsGenome-wide identification of in vivo binding sites of GlxR, a cyclic AMP receptor protein-type regulator in Corynebacterium glutamicum.Allosteric mutants show that PrfA activation is dispensable for vacuole escape but required for efficient spread and Listeria survival in vivoCmr is a redox-responsive regulator of DosR that contributes to M. tuberculosis virulence.Genomic mapping of cAMP receptor protein (CRP Mt) in Mycobacterium tuberculosis: relation to transcriptional start sites and the role of CRPMt as a transcription factor.Regulation of the ahpC gene encoding alkyl hydroperoxide reductase in Mycobacterium smegmatis.Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.Dysregulation of serine biosynthesis contributes to the growth defect of a Mycobacterium tuberculosis crp mutantCyclic AMP signalling in mycobacteria: redirecting the conversation with a common currencyCrystallization 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 nichesDNA Triplexes That Bind Several Cofactor Molecules.Novel structural features drive DNA binding properties of Cmr, a CRP family protein in TB complex mycobacteria.
P2860

Structural Insights into the Mechanism of the Allosteric Transitions of Mycobacterium tuberculosis cAMP Receptor Protein

Item
http://www.wikidata.org/entity/Q27657374
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@ast
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@en
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@nl
type
label
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@ast
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@en
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@nl
prefLabel
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@ast
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@en
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932
P356
P1433
P1476
Structural Insights into the M ...... rculosis cAMP Receptor Protein
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932