1i5o: Difference between revisions

Revision as of 10:27, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1i5o.png

Template:STRUCTURE 1i5o

CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASECRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE

Template:ABSTRACT PUBMED 11323717

About this StructureAbout this Structure

1I5O is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase., Macol CP, Tsuruta H, Stec B, Kantrowitz ER, Nat Struct Biol. 2001 May;8(5):423-6. PMID:11323717

Page seeded by OCA on Tue Jul 1 10:27:35 2008

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OCA

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-'''CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE'''
+===CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE===
-==Overview==
+<!--
-Regulation of protein function, often achieved by allosteric mechanisms, is central to normal physiology and cellular processes. Although numerous models have been proposed to account for the cooperative binding of ligands to allosteric proteins and enzymes, direct structural support has been lacking. Here, we used a combination of X-ray crystallography and small angle X-ray scattering in solution to provide direct structural evidence that the binding of ligand to just one of the six active sites of Escherichia coli aspartate transcarbamoylase induces a concerted structural transition from the T to the R state.
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+{{ABSTRACT_PUBMED_11323717}}
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 [[Category: Pala at the regulatory site]]
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