A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition (Q34682239)

3 August 2017

A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition (English)

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3 August 2017

1 reference

Kimberly A Stieglitz

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3 August 2017

Styliani C Pastra-Landis

2

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3 August 2017

Jiarong Xia

3

1 reference

3 August 2017

Hiro Tsuruta

4

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3 August 2017

Evan R Kantrowitz

5

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3 August 2017

language of work or name

English

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publication date

9 April 2005

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Journal of Molecular Biology

3 August 2017

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3 August 2017

349

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3 August 2017

2

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3 August 2017

413-423

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DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS

3 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

The enzymology of control by feedback inhibition.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

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

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Direct observation of an altered quaternary-structure transition in a mutant aspartate transcarbamoylase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

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

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Escherichia coli aspartate transcarbamylase: the relation between structure and function

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

The conserved residues glutamate-37, aspartate-100, and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase.

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1479453

Aspartate transcarbamylase. Studies of the catalytic subunit by ultraviolet difference spectroscopy

26 October 2018

1 reference

12 December 2020

On the calculation of pKas in proteins

1 reference

12 December 2020

Conformational changes in aspartate trancarbamylase. I. Studies of ligand binding and of subunit interactions by circular dichroism spectroscopy

1 reference

12 December 2020

Ordered substrate binding and evidence for a thermally induced change in mechanism for E. coli aspartate transcarbamylase

1 reference

12 December 2020

The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein Subunits

1 reference

12 December 2020

10.1016/J.JMB.2005.03.073

Identifiers

DOI

1 reference

3 August 2017

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3 August 2017

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