1ahe: Difference between revisions
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|PDB= 1ahe |SIZE=350|CAPTION= <scene name='initialview01'>1ahe</scene>, resolution 2.3Å | |PDB= 1ahe |SIZE=350|CAPTION= <scene name='initialview01'>1ahe</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5 | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <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] | |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= | |GENE= | ||
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[[Category: transferase (aminotransferase)]] | [[Category: transferase (aminotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:07:08 2008'' | ||
Revision as of 09:07, 23 March 2008
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| 1ahe, resolution 2.3Å | |||||||||||||
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| Ligands: | SO4 and PLP | ||||||||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
ASPARTATE AMINOTRANSFERASE HEXAMUTANT
Overview
Mutation of six residues of Escherichia coli aspartate aminotransferase results in substantial acquisition of the transamination properties of tyrosine amino-transferase without loss of aspartate transaminase activity. X-ray crystallographic analysis of key inhibitor complexes of the hexamutant reveals the structural basis for this substrate selectivity. It appears that tyrosine aminotransferase achieves nearly equal affinities for a wide range of amino acids by an unusual conformational switch. An active-site arginine residue either shifts its position to electrostatically interact with charged substrates or moves aside to allow access of aromatic ligands.
About this Structure
1AHE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase., Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN, Nat Struct Biol. 1995 Jul;2(7):548-53. PMID:7664122
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