1ahe: Difference between revisions

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[[Image:1ahe.gif|left|200px]]<br /><applet load="1ahe" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ahe.gif|left|200px]]
caption="1ahe, resolution 2.3&Aring;" />
 
'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''<br />
{{Structure
|PDB= 1ahe |SIZE=350|CAPTION= <scene name='initialview01'>1ahe</scene>, resolution 2.3&Aring;
|SITE=
|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]
|GENE=
}}
 
'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1AHE 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].  
1AHE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHE OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7664122 7664122]
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:[http://www.ncbi.nlm.nih.gov/pubmed/7664122 7664122]
[[Category: Aspartate transaminase]]
[[Category: Aspartate transaminase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: transferase (aminotransferase)]]
[[Category: transferase (aminotransferase)]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:57:33 2008''

Revision as of 10:57, 20 March 2008

File:1ahe.gif


PDB ID 1ahe

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: and
Activity: Aspartate transaminase, with EC number 2.6.1.1
Coordinates: save as pdb, mmCIF, xml



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. 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

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