1pg5: Difference between revisions

Revision as of 10:54, 29 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:1pg5.png

Template:STRUCTURE 1pg5

CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUSCRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUS

Template:ABSTRACT PUBMED 15165857

About this StructureAbout this Structure

1PG5 is a Protein complex structure of sequences from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius., De Vos D, Van Petegem F, Remaut H, Legrain C, Glansdorff N, Van Beeumen JJ, J Mol Biol. 2004 Jun 11;339(4):887-900. PMID:15165857

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OCA

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-'''CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUS'''
+===CRYSTAL STRUCTURE OF THE UNLIGATED (T-STATE) ASPARTATE TRANSCARBAMOYLASE FROM THE EXTREMELY THERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUS===
-==Overview==
+<!--
-Aspartate carbamoyltransferase (ATCase) is a model enzyme for understanding allosteric effects. The dodecameric complex exists in two main states (T and R) that differ substantially in their quaternary structure and their affinity for various ligands. Many hypotheses have resulted from the structure of the Escherichia coli ATCase, but so far other crystal structures to test these have been lacking. Here, we present the tertiary and quaternary structure of the T state ATCase of the hyperthermophilic archaeon Sulfolobus acidocaldarius (SaATC(T)), determined by X-ray crystallography to 2.6A resolution. The quaternary structure differs from the E.coli ATCase, by having altered interfaces between the catalytic (C) and regulatory (R) subunits, and the presence of a novel C1-R2 type interface. Conformational differences in the 240 s loop region of the C chain and the C-terminal region of the R chain affect intersubunit and interdomain interfaces implicated previously in the allosteric behavior of E.coli ATCase. The allosteric-zinc binding domain interface is strengthened at the expense of a weakened R1-C4 type interface. The increased hydrophobicity of the C1-R1 type interface may stabilize the quaternary structure. Catalytic trimers of the S.acidocaldarius ATCase are unstable due to a drastic weakening of the C1-C2 interface. The hyperthermophilic ATCase presents an interesting example of how an allosteric enzyme can adapt to higher temperatures. The structural rearrangement of this thermophilic ATCase may well promote its thermal stability at the expense of changes in the allosteric behavior.
+The line below this paragraph, {{ABSTRACT_PUBMED_15165857}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15165857}}
 ==About this Structure==
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