1fo8: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1fo8.gif|left|200px]]<br /><applet load="1fo8" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1fo8.gif|left|200px]]
caption="1fo8, resolution 1.40&Aring;" />
 
'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''<br />
{{Structure
|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>
|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]
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
1FO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MMC:'>MMC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO8 OCA].  
1FO8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO8 OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11032794 11032794]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11032794 11032794]
[[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]]
[[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
Line 27: Line 36:
[[Category: n-acetylglucosaminyltransferase i]]
[[Category: n-acetylglucosaminyltransferase i]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:50 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:11:48 2008''

Revision as of 12:11, 20 March 2008

File:1fo8.gif


PDB ID 1fo8

Drag the structure with the mouse to rotate
, resolution 1.40Å
Ligands:
Activity: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, with EC number 2.4.1.101
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 Thu Mar 20 11:11:48 2008

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

OCA