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| - | [[Image:9aat.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_9aat| PDB=9aat | SCENE= }} | | {{STRUCTURE_9aat| PDB=9aat | SCENE= }} |
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| - | '''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=== |
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| - | ==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 |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1593633 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1593633}} |
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| | ==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 22:52:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 12:58:28 2008'' |
Revision as of 09:58, 11 July 2008
Template:STRUCTURE 9aat
X-RAY STRUCTURE REFINEMENT AND COMPARISON OF THREE FORMS OF MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE
Template:ABSTRACT PUBMED 1593633
About this Structure
9AAT 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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