1ahe: Difference between revisions

Revision as of 16:51, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ahe.png

Template:STRUCTURE 1ahe

ASPARTATE AMINOTRANSFERASE HEXAMUTANTASPARTATE AMINOTRANSFERASE HEXAMUTANT

Template:ABSTRACT PUBMED 7664122

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

Page seeded by OCA on Mon Jun 30 16:51:25 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ahe.gif|left|200px]]
+{{Seed}}
+[[Image:1ahe.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ahe|  PDB=1ahe  |  SCENE=  }}
-'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7664122}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7664122 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7664122}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Jansonius, J N.]]
 [[Category: Malashkevich, V N.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:16:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:51:25 2008''