1ahe: Difference between revisions

Revision as of 12:44, 21 February 2008

ASPARTATE AMINOTRANSFERASE HEXAMUTANT

OverviewOverview

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 StructureAbout this Structure

1AHE is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Aspartate transaminase, with EC number 2.6.1.1 Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 11:44:30 2008

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OCA

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-[[Image:1ahe.gif|left|200px]]<br /><applet load="1ahe" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ahe.gif|left|200px]]<br /><applet load="1ahe" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ahe, resolution 2.3&Aring;" />
 '''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''<br />
 ==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.
+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==
-AHE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AHE OCA].
+AHE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHE OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Jansonius, J.N.]]
+[[Category: Jansonius, J N.]]
-[[Category: Malashkevich, V.N.]]
+[[Category: Malashkevich, V N.]]
 [[Category: PLP]]
 [[Category: SO4]]
 [[Category: transferase (aminotransferase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:51:20 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:30 2008''