8aat
From Proteopedia
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X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE
Overview
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.
About this Structure
8AAT is a Single protein structure of sequence from Gallus gallus with PLP as ligand. Active as Aspartate transaminase, with EC number 2.6.1.1 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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