8aat: Difference between revisions
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[[Image:8aat.gif|left|200px]] | [[Image:8aat.gif|left|200px]] | ||
'''X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE''' | {{Structure | ||
|PDB= 8aat |SIZE=350|CAPTION= <scene name='initialview01'>8aat</scene>, resolution 2.3Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | |||
|GENE= | |||
}} | |||
'''X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
8AAT is a [ | 8AAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AAT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1593633 1593633] | ||
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
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[[Category: transferase(aminotransferase)]] | [[Category: transferase(aminotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:15:13 2008'' | ||
Revision as of 17:15, 20 March 2008
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| 8aat, resolution 2.3Å | |||||||||||||
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| Ligands: | PLP | ||||||||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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