The Allosteric activator Mg-ATP Modifies the Quaternary Structure of the R-state of Escherichia coli Aspartate Transcarbamylase Without Altering the T↔R Equilibrium-Reference-Cited by-同舟云学术

The Allosteric activator Mg-ATP Modifies the Quaternary Structure of the R-state of Escherichia coli Aspartate Transcarbamylase Without Altering the T↔R Equilibrium

Published:2001-06 Issue:3 Volume:309 Page:817-832
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Fetler L.,Vachette P.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference68 articles.

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4. New structures of allosteric proteins revealing remarkable conformational changes;Mattevi;Curr. Opin. Struct. Biol,1996

5. Aspartate transcarbamylase from Escherichia coli;Hervé,1989

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