We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1v84

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1v84.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1v84.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1v84| PDB=1v84 | SCENE= }}
{{STRUCTURE_1v84| PDB=1v84 | SCENE= }}
-
'''Crystal structure of human GlcAT-P in complex with N-acetyllactosamine, Udp, and Mn2+'''
+
===Crystal structure of human GlcAT-P in complex with N-acetyllactosamine, Udp, and Mn2+===
-
==Overview==
+
<!--
-
The HNK-1 carbohydrate epitope is found on many neural cell adhesion molecules. Its structure is characterized by a terminal sulfated glucuronyl acid. The glucuronyltransferases, GlcAT-P and GlcAT-S, are involved in the biosynthesis of the HNK-1 epitope, GlcAT-P as the major enzyme. We overexpressed and purified the recombinant human GlcAT-P from Escherichia coli. Analysis of its enzymatic activity showed that it catalyzed the transfer reaction for N-acetyllactosamine (Galbeta1-4GlcNAc) but not lacto-N-biose (Galbeta1-3GlcNAc) as an acceptor substrate. Subsequently, we determined the first x-ray crystal structures of human GlcAT-P, in the absence and presence of a donor substrate product UDP, catalytic Mn(2+), and an acceptor substrate analogue N-acetyllactosamine (Galbeta1-4GlcNAc) or an asparagine-linked biantennary nonasaccharide. The asymmetric unit contains two independent molecules. Each molecule is an alpha/beta protein with two regions that constitute the donor and acceptor substrate binding sites. The UDP moiety of donor nucleotide sugar is recognized by conserved amino acid residues including a DXD motif (Asp(195)-Asp(196)-Asp(197)). Other conserved amino acid residues interact with the terminal galactose moiety of the acceptor substrate. In addition, Val(320) and Asn(321), which are located on the C-terminal long loop from a neighboring molecule, and Phe(245) contribute to the interaction with GlcNAc moiety. These three residues play a key role in establishing the acceptor substrate specificity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14993226}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14993226 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14993226}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Hnk-1 epitope]]
[[Category: Hnk-1 epitope]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:12:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:16:45 2008''

Revision as of 05:16, 29 July 2008

Image:1v84.png

Template:STRUCTURE 1v84

Crystal structure of human GlcAT-P in complex with N-acetyllactosamine, Udp, and Mn2+

Template:ABSTRACT PUBMED 14993226

About this Structure

1V84 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1., Kakuda S, Shiba T, Ishiguro M, Tagawa H, Oka S, Kajihara Y, Kawasaki T, Wakatsuki S, Kato R, J Biol Chem. 2004 May 21;279(21):22693-703. Epub 2004 Mar 1. PMID:14993226

Page seeded by OCA on Tue Jul 29 08:16:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v84"
Personal tools