1fo8: Difference between revisions

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Revision as of 20:26, 30 March 2008

File:1fo8.gif

, resolution 1.40Å

Ligands:

Activity:

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, with EC number 2.4.1.101

Related:

1FO9, 1FOA

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I

OverviewOverview

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.

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 Sun Mar 30 20:26:53 2008

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

OCA

@@ Line 4: / Line 4: @@
 |PDB= 1fo8 |SIZE=350|CAPTION= <scene name='initialview01'>1fo8</scene>, resolution 1.40&Aring;
 |SITE=
-|LIGAND= <scene name='pdbligand=MMC:METHYL MERCURY ION'>MMC</scene>
+|LIGAND= <scene name='pdbligand=MMC:METHYL+MERCURY+ION'>MMC</scene>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-1,3-mannosyl-glycoprotein_2-beta-N-acetylglucosaminyltransferase Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.101 2.4.1.101]
+|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-1,3-mannosyl-glycoprotein_2-beta-N-acetylglucosaminyltransferase Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.101 2.4.1.101] </span>
 |GENE=
+|DOMAIN=
+|RELATEDENTRY=[[1fo9|1FO9]], [[1foa|1FOA]]
+|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo8 OCA], [http://www.ebi.ac.uk/pdbsum/1fo8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fo8 RCSB]</span>
 }}
@@ Line 29: / Line 32: @@
 [[Category: Yuwaraj, S.]]
 [[Category: Zhou, S.]]
-[[Category: MMC]]
+[[Category: alpha-1,3-mannosyl-glycoprotein beta-1,2-n-acetylglucosaminyltransferase]]
-[[Category: 2-n-acetylglucosaminyltransferase]]
-[[Category: 3-mannosyl-glycoprotein beta-1]]
-[[Category: alpha-1]]
 [[Category: methylmercury derivative]]
 [[Category: n-acetylglucosaminyltransferase i]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:53 2008''