This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1omz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1omz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1omz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1omz| PDB=1omz | SCENE= }}
{{STRUCTURE_1omz| PDB=1omz | SCENE= }}
-
'''crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) in complex with UDPGalNAc'''
+
===crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) in complex with UDPGalNAc===
-
==Overview==
+
<!--
-
EXTL2, an alpha1,4-N-acetylhexosaminyltransferase, catalyzes the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta1-3[galactose]beta1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. We have solved the x-ray crystal structure of the catalytic domain of mouse EXTL2 in the apo-form and with donor substrates UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine. In addition, a structure of the ternary complex with UDP and the acceptor substrate analog [glucuronic acid]beta1-3[galactose]beta1-O-naphthalenemethanol has been determined. These structures reveal three highly conserved residues, Asn-243, Asp-246, and Arg-293, located at the active site. Mutation of these residues greatly decreases the activity. In the ternary complex, an interaction exists between the beta-phosphate of the UDP leaving group and the acceptor hydroxyl of the substrate that may play a functional role in catalysis. These structures represent the first structures from the exostosin gene family and provide important insight into the mechanisms of alpha1,4-N-acetylhexosaminyl transfer in heparan biosynthesis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12562774}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12562774 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12562774}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Dxd motif]]
[[Category: Dxd motif]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:02:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:32:24 2008''

Revision as of 21:32, 27 July 2008

Image:1omz.png

Template:STRUCTURE 1omz

crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) in complex with UDPGalNAc

Template:ABSTRACT PUBMED 12562774

About this Structure

1OMZ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis., Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M, J Biol Chem. 2003 Apr 18;278(16):14420-8. Epub 2003 Jan 31. PMID:12562774

Page seeded by OCA on Mon Jul 28 00:32:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1omz"
Personal tools