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.


2apc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2apc.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2apc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2apc| PDB=2apc | SCENE= }}
{{STRUCTURE_2apc| PDB=2apc | SCENE= }}
-
'''Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP-GlcNAc phosphonate'''
+
===Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP-GlcNAc phosphonate===
-
==Overview==
+
<!--
-
The Golgi-resident glycosyltransferase, UDP-N-acetyl-d-glucosamine:alpha-3-d-mannoside beta-1,2-N-acetylglucosaminyltransferase I (GnT I), initiates the conversion of high-mannose oligosaccharides to complex and hybrid structures in the biosynthesis of N-linked glycans. Reported here are the X-ray crystal structures of GnT I in complex with UDP-CH2-GlcNAc (a non-hydrolyzable C-glycosidic phosphonate), UDP-2-deoxy-2-fluoro-glucose, UDP-glucose and UDP. Collectively, these structures provide evidence for the importance of the GlcNAc moiety and its N-acetyl group in donor substrate binding, as well as insight into the role played by the flexible 318-330 loop in substrate binding and product release. In addition, the UDP-CH2-GlcNAc complex reveals a well-defined glycerol molecule poised for nucleophilic attack on the C1 atom of the donor substrate analogue. The position and orientation of this glycerol molecule have allowed us to model the binding of the Manalpha1,3Manbeta1 moiety of the acceptor substrate and, based on the model, to suggest a rationalization for the main determinants of GnT I acceptor specificity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16769084}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16769084 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16769084}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Udp-glcnac]]
[[Category: Udp-glcnac]]
[[Category: Udp-glcnac phosphonate]]
[[Category: Udp-glcnac phosphonate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:18:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:51:38 2008''

Revision as of 14:51, 27 July 2008

Image:2apc.png


PDB ID 2apc

Drag the structure with the mouse to rotate
2apc, resolution 1.50Å ()
Ligands: , ,
Activity: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, with EC number 2.4.1.101
Related: 1foa, 1fo9, 1fo8
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of N-Acetylglucosaminyltransferase I in Complex with UDP-GlcNAc phosphonate

Template:ABSTRACT PUBMED 16769084

About this Structure

2APC is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues., Gordon RD, Sivarajah P, Satkunarajah M, Ma D, Tarling CA, Vizitiu D, Withers SG, Rini JM, J Mol Biol. 2006 Jun 30;360(1):67-79. Epub 2006 May 12. PMID:16769084

Page seeded by OCA on Sun Jul 27 17:51:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2apc"
Personal tools