The role of loops 3 and 4 in the interdomains and intersubunits communication of E. coli cAMP receptor protein

Shen, Xianrong; Tao, Wenbing; Kong, Jilie; Yu, Shaoning

doi:10.1016/j.ijbiomac.2008.01.006

Cited by 5 publications

(11 citation statements)

References 32 publications

(55 reference statements)

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“…On the basis of screening mutations in the loops (deletion in loop 3, insertion in loop 4 and the combined mutations), it has been found that these loops can play important roles in the function of CRP [Chen and Ching Lee, 2003]. Loop 3 is involved in intersubunit signal communication, whereas loop 4 is involved in the cAMP-binding pocket and interdomain signal transmission [Shen et al, 2008].…”

Section: Cyclic Amp Binding By Crpmentioning

confidence: 99%

cAMP Receptor Protein from <i>Escherichia coli</i> as a Model of Signal Transduction in Proteins – A Review

Fic¹,

Bonarek²,

Górecki³

et al. 2008

Microb Physiol

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In Escherichia coli, cyclic AMP receptor protein (CRP) is known to regulate the transcription of about 100 genes. The signal to activate CRP is the binding of cyclic AMP. It has been suggested that binding of cAMP to CRP leads to a long-distance signal transduction from the N-terminal cAMP-binding domain to the C-terminal domain of the protein, which is responsible for interaction with specific sequences of DNA. The signal transduction plays a crucial role in the activation of the protein. The most sophisticated spectroscopic techniques, other techniques frequently used in structural biochemistry, and site-directed mutagenesis have been used to investigate the details of cAMP-mediated allosteric control over CRP conformation and activity as a transcription factor. The aim of this review is to summarize recent works and developments pertaining to cAMP-dependent CRP signal transduction in E. coli.

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Section: Cyclic Amp Binding By Crpmentioning

confidence: 99%

cAMP Receptor Protein from <i>Escherichia coli</i> as a Model of Signal Transduction in Proteins – A Review

Fic¹,

Bonarek²,

Górecki³

et al. 2008

Microb Physiol

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“…These proteins have diverse sequences and functions, but all consist of a cAMP-binding motif, share a common structural architecture, and are involved in diverse cellular functions [1][2][3][4][5][6][7]. CRP from E. coli has been studied extensively in fields ranging from molecular dynamics [8] and bioinformatics [9], to biochemistry [3] and biophysics [10] in order to understand the allostery induced by cAMP binding, and it has been used as a model system to investigate the allosteric mechanism induced by cAMP binding [11,12].…”

Section: Introductionmentioning

confidence: 99%

“…1) [13][14][15]. On the basis of structural data, the cAMP-binding motif of CRP is mainly located in the eightstrand ␤-roll with a helix forming the back of the binding pocket [7,11,12]. cAMP plays a central role in controlling the catabolic activity of both prokaryotic and eukaryotic cells [16].…”

Section: Introductionmentioning

confidence: 99%

“…The binding of cAMP induces conformational changes, including subunit realignment and domain reorientation leading to the activation of CRP [17]. Previous works have shown that loops 3 and 4 of CRP not only serve as connectors, but also play functional roles in the intact CRP [11,12]. CRP loop 3 is assumed to be involved in both interdomain and intersubunit interactions, and to modulate the binding affinity of cAMP and DNA [11].…”

Section: Introductionmentioning

confidence: 99%

“…Our laboratory previously designed two CRP mutants: insertion mutant iCRP with a KGSKM insertion between the residues 78 and 79, and insertion-deletion mutant idCRP with a KGSKM insertion between the residues 78 and 79 plus deletion of the residues 54-56 (EEG) in loop 3. The mutants were used to investigate the thermodynamics of the interaction between CRP and cAMP [12]. Loops 3 and 4 of CRP were found to play important functional roles in CRP.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein

Gao

et al. 2012

International Journal of Biological Macromolecules

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Survey of the year 2008: applications of isothermal titration calorimetry

Falconer

Penkova

Jelesarov

et al. 2010

J of Molecular Recognition

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Isothermal titration calorimetry (ITC) is a fast, accurate and label-free method for measuring the thermodynamics and binding affinities of molecular associations in solution. Because the method will measure any reaction that results in a heat change, it is applicable to many different fields of research from biomolecular science, to drug design and materials engineering, and can be used to measure binding events between essentially any type of biological or chemical ligand. ITC is the only method that can directly measure binding energetics including Gibbs free energy, enthalpy, entropy and heat capacity changes. Not only binding thermodynamics but also catalytic reactions, conformational rearrangements, changes in protonation and molecular dissociations can be readily quantified by performing only a small number of ITC experiments. In this review, we highlight some of the particularly interesting reports from 2008 employing ITC, with a particular focus on protein interactions with other proteins, nucleic acids, lipids and drugs. As is tradition in these reviews we have not attempted a comprehensive analysis of all 500 papers using ITC, but emphasize those reports that particularly captured our interest and that included more thorough discussions we consider exemplify the power of the technique and might serve to inspire other users.

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The role of loops 3 and 4 in the interdomains and intersubunits communication of E. coli cAMP receptor protein

Cited by 5 publications

References 32 publications

cAMP Receptor Protein from <i>Escherichia coli</i> as a Model of Signal Transduction in Proteins – A Review

cAMP Receptor Protein from <i>Escherichia coli</i> as a Model of Signal Transduction in Proteins – A Review

Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein

Survey of the year 2008: applications of isothermal titration calorimetry

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