1ahg

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[[Image:1ahg.gif|left|200px]]
[[Image:1ahg.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ahg |SIZE=350|CAPTION= <scene name='initialview01'>1ahg</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1ahg", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1ahg| PDB=1ahg | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ahg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahg OCA], [http://www.ebi.ac.uk/pdbsum/1ahg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ahg RCSB]</span>
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}}
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'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''
'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''
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[[Category: Jansonius, J N.]]
[[Category: Jansonius, J N.]]
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
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[[Category: transferase (aminotransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:51:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:40:16 2008''
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Revision as of 10:51, 30 April 2008

Image:1ahg.gif

Template:STRUCTURE 1ahg

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

1AHG 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 Page seeded by OCA on Wed Apr 30 13:51:34 2008

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