1ahf: Difference between revisions

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[[Image:1ahf.gif|left|200px]]
[[Image:1ahf.gif|left|200px]]


{{Structure
<!--
|PDB= 1ahf |SIZE=350|CAPTION= <scene name='initialview01'>1ahf</scene>, resolution 2.3&Aring;
The line below this paragraph, containing "STRUCTURE_1ahf", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=IOP:INDOLYLPROPIONIC+ACID'>IOP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1ahf| PDB=1ahf  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ahf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahf OCA], [http://www.ebi.ac.uk/pdbsum/1ahf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ahf RCSB]</span>
}}


'''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.]]
[[Category: transferase (aminotransferase)]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:16:27 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:40:20 2008''

Revision as of 10:16, 2 May 2008

File:1ahf.gif

Template:STRUCTURE 1ahf

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

1AHF 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 Page seeded by OCA on Fri May 2 10:16:27 2008

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