Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

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Gly184 of the Escherichia coli cAMP receptor protein provides optimal context for both DNA binding and RNA polymerase interaction.Evolution of gene knockout strains of E. coli reveal regulatory architectures governed by metabolism

P2860

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Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

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http://www.wikidata.org/entity/Q36283704

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Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

@ast

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

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type

Item

label

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

@ast

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

@en

prefLabel

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

@ast

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

@en

P1476

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket

@en

P2093

Cameron V Saunders

http://www.w3.org/2001/XMLSchema#string

Cory L Brooks

http://www.w3.org/2001/XMLSchema#string

Hwan Youn

http://www.w3.org/2001/XMLSchema#string

Jin Park

http://www.w3.org/2001/XMLSchema#string

Jose Serate

http://www.w3.org/2001/XMLSchema#string

Joy J Goto

http://www.w3.org/2001/XMLSchema#string

Matt N Hicks

http://www.w3.org/2001/XMLSchema#string

Sanjiva M Gunasekara

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Simranjeet K Grover

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P2860

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

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

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

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

Crystal Structure of the Pseudomonas aeruginosa Virulence Factor Regulator

A general method applicable to the search for similarities in the amino acid sequence of two proteins

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

Transcription activation by catabolite activator protein (CAP)

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

Transcription activation mediated by a cyclic AMP receptor protein from Thermus thermophilus HB8

P304

26587-26596

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scholarly article

P356

10.1074/JBC.M115.678474

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English

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http://www.w3.org/2001/XMLSchema#string

P478

290

http://www.w3.org/2001/XMLSchema#string

P50

Jin-Won Lee

P577

2015-09-16T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

26378231

http://www.w3.org/2001/XMLSchema#string

P921

directed evolution

protein evolution

P932

4646316

http://www.w3.org/2001/XMLSchema#string

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

about

P2860

P2860

Directed evolution of the Escherichia coli cAMP receptor protein at the cAMP pocket.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

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P50

P577

P698

P921

P932

P356

P1433

P1476

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P356

P407

P433

P478

P50

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P698

P921

P932