3tat: Difference between revisions

Line 1:

[[Image:3tat.~~jpg~~|left|200px]]

[[Image:3tat.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~TYROSINE AMINOTRANSFERASE FROM E. COLI~~'''~~

===TYROSINE AMINOTRANSFERASE FROM E. COLI===

~~==Overview==~~

<!--

~~Tyrosine aminotransferase catalyzes transamination for both dicarboxylic and aromatic amino~~-~~acid substrates. The substrate~~-free Escherichia coli tyrosine aminotransferase (eTAT) bound with the cofactor pyridoxal 5'-phosphate (PLP) was crystallized in the trigonal space group P3(2). A low-resolution crystal structure of eTAT was determined by molecular-replacement methods. The ~~overall folding of eTAT resembles that of the aspartate aminotransferases~~, ~~with~~ the ~~two identical subunits forming a dimer in which each monomer binds a PLP molecule via a covalent bond linked~~ to the ~~epsilon-NH~~(2) ~~group of Lys258. Comparison of the structure of eTAT with those of the open~~, ~~half-open or closed form of chicken or E. coli aspartate aminotransferases shows the eTAT structure to be in~~ the ~~open conformation~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10417420}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10417420 is the PubMed ID number.

-->

==About this Structure==

Line 31:

Line 35:

[[Category: Aromatic substrate]]

[[Category: Plp enzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:13:37 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:08:15 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:3tat.jpg|left|200px]]
+{{Seed}}
+[[Image:3tat.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3tat|  PDB=3tat  |  SCENE=  }}
-'''TYROSINE AMINOTRANSFERASE FROM E. COLI'''
+===TYROSINE AMINOTRANSFERASE FROM E. COLI===
-==Overview==
+<!--
-Tyrosine aminotransferase catalyzes transamination for both dicarboxylic and aromatic amino-acid substrates. The substrate-free Escherichia coli tyrosine aminotransferase (eTAT) bound with the cofactor pyridoxal 5'-phosphate (PLP) was crystallized in the trigonal space group P3(2). A low-resolution crystal structure of eTAT was determined by molecular-replacement methods. The overall folding of eTAT resembles that of the aspartate aminotransferases, with the two identical subunits forming a dimer in which each monomer binds a PLP molecule via a covalent bond linked to the epsilon-NH(2) group of Lys258. Comparison of the structure of eTAT with those of the open, half-open or closed form of chicken or E. coli aspartate aminotransferases shows the eTAT structure to be in the open conformation.
+The line below this paragraph, {{ABSTRACT_PUBMED_10417420}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10417420 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10417420}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Aromatic substrate]]
 [[Category: Plp enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:13:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 13:08:15 2008''