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Structural basis of the allosteric behaviour of phosphofructokinase

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Structural basis of the allosteric behaviour of phosphofructokinase (English)

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author name string

T Schirmer

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1

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P R Evans

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2

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language of work or name

English

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publication date

11 January 1990

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published in

Nature

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volume

343

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page(s)

140-5

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issue

6254

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cites work

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

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Escherichia coli aspartate transcarbamylase: the relation between structure and function

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The allosteric transition of glycogen phosphorylase

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Kinetics of the allosteric interactions of phosphofructokinase from Escherichia coli

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Structure and control of phosphofructokinase from Bacillus stearothermophilus

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Phosphofructokinase: structure and control

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Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products

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Crystal structure of unliganded phosphofructokinase from Escherichia coli

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Crystallographic structure of allosterically inhibited phosphofructokinase at 7 A resolution

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7 January 2021

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Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene

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7 January 2021

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Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase.

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7 January 2021

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Improved Fourier coefficients for maps using phases from partial structures with errors

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7 January 2021

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Mechanisms of domain closure in proteins

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Identifiers

DOI

10.1038/343140A0

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Dimensions Publication ID

1052534096

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PubMed ID

2136935

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Springer Nature article ID

10.1038/343140a0

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(Q27666870)

Structural basis of the allosteric behaviour of phosphofructokinase

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