X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase☆
作者： Catherine A. McPhalen , Michael G. Vincent , Johan N. Jansonius
DOI: 10.1016/0022-2836(92)90935-D
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摘要: The X-ray crystal structures of three forms the enzyme aspartate aminotransferase (EC 2.6.1.1) from chicken heart mitochondria have been refined by least-squares methods: holoenzyme with co-factor pyridoxal-5'-phosphate bound at pH 7.5 (1.9 A resolution), 5.1 (2.3 resolution) and pyridoxamine-5'-phosphate (2.2 resolution). crystallographic agreement factors [formula: see text] for are 0.166, 0.130 0.131, respectively, all data in resolution range 10.0 to limit diffraction each structure. secondary, super-secondary domain pyridoxal-phosphate described detail. surface area interface between monomer subunits this dimeric alpha 2 protein is unusually large, indicating a very stable dimer. This consistent biochemical data. Both subunit interfaces relatively smooth compared other proteins. interactions its among structures. Observed changes conformation may be related spectral energetics catalytic reaction. Small but significant adjustments seen. These accommodated small rigid-body shifts secondary structural elements, packing defects core.
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