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[[Image:8aat.gif|left|200px]]
{{Seed}}
[[Image:8aat.png|left|200px]]


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{{STRUCTURE_8aat|  PDB=8aat  |  SCENE=  }}  
{{STRUCTURE_8aat|  PDB=8aat  |  SCENE=  }}  


'''X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE'''
===X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE===




==Overview==
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The X-ray crystal structures of three forms of the enzyme aspartate aminotransferase (EC 2.6.1.1) from chicken heart mitochondria have been refined by least-squares methods: holoenzyme with the co-factor pyridoxal-5'-phosphate bound at pH 7.5 (1.9 A resolution), holoenzyme with pyridoxal-5'-phosphate bound at pH 5.1 (2.3 A resolution) and holoenzyme with the co-factor pyridoxamine-5'-phosphate bound at pH 7.5 (2.2 A resolution). The crystallographic agreement factors [formula: see text] for the structures are 0.166, 0.130 and 0.131, respectively, for all data in the resolution range from 10.0 A to the limit of diffraction for each structure. The secondary, super-secondary and domain structures of the pyridoxal-phosphate holoenzyme at pH 7.5 are described in detail. The surface area of the interface between the monomer subunits of this dimeric alpha 2 protein is unusually large, indicating a very stable dimer. This is consistent with biochemical data. Both subunit and domain interfaces are relatively smooth compared with other proteins. The interactions of the protein with its co-factor are described and compared among the three structures. Observed changes in co-factor conformation may be related to spectral changes and the energetics of the catalytic reaction. Small but significant adjustments of the protein to changes in co-factor conformation are seen. These adjustments may be accommodated by small rigid-body shifts of secondary structural elements, and by packing defects in the protein core.
The line below this paragraph, {{ABSTRACT_PUBMED_1593633}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_1593633}}


==About this Structure==
==About this Structure==
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[[Category: Mcphalen, C A.]]
[[Category: Mcphalen, C A.]]
[[Category: Vincent, M G.]]
[[Category: Vincent, M G.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:48:21 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 12:59:11 2008''

Revision as of 09:59, 11 July 2008

File:8aat.png

Template:STRUCTURE 8aat

X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE

Template:ABSTRACT PUBMED 1593633

About this Structure

8AAT is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase., McPhalen CA, Vincent MG, Jansonius JN, J Mol Biol. 1992 May 20;225(2):495-517. PMID:1593633

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