1tat: Difference between revisions

Revision as of 17:56, 27 July 2008

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File:1tat.png

Template:STRUCTURE 1tat

CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONSCRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS

Template:ABSTRACT PUBMED 8120903

About this StructureAbout this Structure

1TAT is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Crystalline mitochondrial aspartate aminotransferase exists in only two conformations., Hohenester E, Jansonius JN, J Mol Biol. 1994 Mar 4;236(4):963-8. PMID:8120903

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OCA

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-'''CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS'''
+===CRYSTALLINE MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE EXISTS IN ONLY TWO CONFORMATIONS===
-==Overview==
+<!--
-The subunits of the alpha 2-dimeric enzyme aspartate aminotransferase are composed of two distinct domains, one large and one small. The active sites are situated close to both the intersubunit and the interdomain interface. Binding of substrate analogues to the active site induces a large conformational change in the enzyme, whereby the small domain rotates by 13 degrees relative to the large domain and completely buries the ligand. We have determined the crystal structures of chicken mitochondrial aspartate aminotransferase (mAATase) in two new crystal forms. A comparison of the structures of mAATase in five crystal forms, including both the unliganded and the liganded enzyme, shows that mAATase exists in either one of two unique conformations, with only minimal adaptations to the crystal lattice. This suggests that both the open, unliganded and closed, liganded structure of mAATase are, to a large extent, stabilized by intramolecular interactions, and are consequently representative of functional states of the protein in solution. A 2-fold-symmetric packing interaction between small domains occurring identically in three crystal forms of mAATase is described.
+The line below this paragraph, {{ABSTRACT_PUBMED_8120903}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8120903 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8120903}}
 ==About this Structure==
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 [[Category: Jansonius, J N.]]
 [[Category: Aminotransferase]]
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