1foa: Difference between revisions

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|PDB= 1foa |SIZE=350|CAPTION= <scene name='initialview01'>1foa</scene>, resolution 1.80&Aring;
|PDB= 1foa |SIZE=350|CAPTION= <scene name='initialview01'>1foa</scene>, resolution 1.80&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1fo8|1FO8]], [[1fo9|1FO9]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1foa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1foa OCA], [http://www.ebi.ac.uk/pdbsum/1foa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1foa RCSB]</span>
}}
}}


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[[Category: Yuwaraj, S.]]
[[Category: Yuwaraj, S.]]
[[Category: Zhou, S.]]
[[Category: Zhou, S.]]
[[Category: GOL]]
[[Category: alpha-1,3-mannosyl-glycoprotein]]
[[Category: MN]]
[[Category: beta-1,2-n-acetylglucosaminyltransferase]]
[[Category: UD1]]
[[Category: 2-n-acetylglucosaminyltransferase]]
[[Category: 3-mannosyl-glycoprotein]]
[[Category: alpha-1]]
[[Category: beta-1]]
[[Category: donor substrate and metal ion complex]]
[[Category: donor substrate and metal ion complex]]
[[Category: n-acetylglucosaminyltransferase i]]
[[Category: n-acetylglucosaminyltransferase i]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:46 2008''
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Revision as of 20:26, 30 March 2008

File:1foa.gif


PDB ID 1foa

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: , ,
Activity: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, with EC number 2.4.1.101
Related: 1FO8, 1FO9


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

1FOA 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

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