1fo8: Difference between revisions

Revision as of 03:40, 1 July 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:1fo8.png

Template:STRUCTURE 1fo8

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE ICRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I

Template:ABSTRACT PUBMED 11032794

About this StructureAbout this Structure

1FO8 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily., Unligil UM, Zhou S, Yuwaraj S, Sarkar M, Schachter H, Rini JM, EMBO J. 2000 Oct 16;19(20):5269-80. PMID:11032794

Page seeded by OCA on Tue Jul 1 03:40:13 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fo8.gif|left|200px]]
+{{Seed}}
+[[Image:1fo8.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1fo8|  PDB=1fo8  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''
+===CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I===
-==Overview==
+<!--
-N:-acetylglucosaminyltransferase I (GnT I) serves as the gateway from oligomannose to hybrid and complex N:-glycans and plays a critical role in mammalian development and possibly all metazoans. We have determined the X-ray crystal structure of the catalytic fragment of GnT I in the absence and presence of bound UDP-GlcNAc/Mn(2+) at 1.5 and 1.8 A resolution, respectively. The structures identify residues critical for substrate binding and catalysis and provide evidence for similarity, at the mechanistic level, to the deglycosylation step of retaining beta-glycosidases. The structuring of a 13 residue loop, resulting from UDP-GlcNAc/Mn(2+) binding, provides an explanation for the ordered sequential 'Bi Bi' kinetics shown by GnT I. Analysis reveals a domain shared with Bacillus subtilis glycosyltransferase SpsA, bovine beta-1,4-galactosyl transferase 1 and Escherichia coli N:-acetylglucosamine-1-phosphate uridyltransferase. The low sequence identity, conserved fold and related functional features shown by this domain define a superfamily whose members probably share a common ancestor. Sequence analysis and protein threading show that the domain is represented in proteins from several glycosyltransferase families.
+The line below this paragraph, {{ABSTRACT_PUBMED_11032794}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11032794 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11032794}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Methylmercury derivative]]
 [[Category: N-acetylglucosaminyltransferase i]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:34:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:40:13 2008''