Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. (Q27654627)

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25 January 2020

title

Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (English)

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25 January 2020

4

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25 January 2020

author name string

Nataliya Popovych

1

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25 January 2020

Shiou-Ru Tzeng

2

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25 January 2020

Marco Tonelli

3

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25 January 2020

Charalampos G Kalodimos

5

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25 January 2020

language of work or name

English

0 references

publication date

9 April 2009

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

25 January 2020

published in

1 reference

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25 January 2020

volume

106

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25 January 2020

issue

17

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25 January 2020

page(s)

6927-6932

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

25 January 2020

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20 March 2017

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Catabolite activator protein: DNA binding and transcription activation

20 March 2017

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Structural basis for modulation and agonist specificity of HCN pacemaker channels

20 March 2017

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Structure and regulation of the cAMP-binding domains of Epac2

20 March 2017

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Structural basis of transcription activation: the CAP-alpha CTD-DNA complex

20 March 2017

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Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution

20 March 2017

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Structure of the CO sensing transcription activator CooA

20 March 2017

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Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface

20 March 2017

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

20 March 2017

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Weak alignment NMR: a hawk-eyed view of biomolecular structure

22 April 2017

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Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees

20 March 2017

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Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA

20 March 2017

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Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data

20 March 2017

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Structural specificity in coiled-coil interactions.

7 April 2017

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Two-state allosteric modeling suggests protein equilibrium as an integral component for cyclic AMP (cAMP) specificity in the cAMP receptor protein of Escherichia coli

29 September 2017

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Evolution of allostery in the cyclic nucleotide binding module

29 September 2017

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Proline cis-trans isomerization controls autoinhibition of a signaling protein

29 September 2017

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Dynamically driven protein allostery.

29 September 2017

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Study of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein

29 September 2017

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The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif.

29 September 2017

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Solution NMR-derived global fold of a monomeric 82-kDa enzyme

29 September 2017

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The cAMP binding domain: an ancient signaling module

29 September 2017

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Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs

29 September 2017

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Identifying global regulators in transcriptional regulatory networks in bacteria

29 September 2017

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Allosteric regulation of the cAMP receptor protein

29 September 2017

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Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.

29 September 2017

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Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation

29 September 2017

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Sites of allosteric shift in the structure of the cyclic AMP receptor protein.

29 September 2017

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Stoichiometry and structural effect of the cyclic nucleotide binding to cyclic AMP receptor protein.

19 June 2018

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Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0900595106

Interplay between site-specific mutations and cyclic nucleotides in modulating DNA recognition by Escherichia coli cyclic AMP receptor protein.

21 January 2018

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Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0900595106

Analogs of cyclic AMP that elicit the biochemically defined conformational change in catabolite gene activator protein (CAP) but do not stimulate binding to DNA

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19359484

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Fluorescence study of Escherichia coli cyclic AMP receptor protein

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19359484

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Structural understanding of the allosteric conformational change of cyclic AMP receptor protein by cyclic AMP binding

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19359484

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.0900595106

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19359484%20AND%20SRC:MED&resulttype=core&format=json

25 January 2020

0 references

1 reference

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25 January 2020

PubMed publication ID

19359484

1 reference