The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase (Q44193826)

30 November 2017

title

The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase (English)

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30 November 2017

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Robin S Chan

1

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30 November 2017

Jessica B Sakash

2

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30 November 2017

Christine P Macol

3

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30 November 2017

Jay M West

4

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30 November 2017

Hiro Tsuruta

5

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30 November 2017

Evan R Kantrowitz

6

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30 November 2017

language of work or name

English

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publication date

23 October 2002

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Journal of Biological Chemistry

30 November 2017

published in

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30 November 2017

volume

277

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30 November 2017

issue

51

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30 November 2017

page(s)

49755-49760

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Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.

30 November 2017

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Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions

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Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH

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A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies.

21 January 2018

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Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.

21 January 2018

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The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain

21 January 2018

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Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase.

21 January 2018

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Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase.

21 January 2018

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A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase

21 January 2018

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The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase

21 January 2018

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Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase

21 January 2018

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NEGATIVE AND POSITIVE ION MASS ANALYSIS OF DICARBOXYLIC ACIDS IN STUDIES ON THE MECHANISM OF THE METHYLMALONYL ISOMERASE REACTION

21 January 2018

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The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects

21 January 2018

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An improved colorimetric assay for aspartate and ornithine transcarbamylases

21 January 2018

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Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions

21 January 2018

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Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

21 January 2018

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Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding

21 January 2018

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Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylase

21 January 2018

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Kinetic consequences of site-specific mutation of Glu-239----Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzyme

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M208919200

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30 November 2017

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