1foa: Difference between revisions

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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 with , and as ligands. Active as Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, with EC number 2.4.1.101 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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-[[Image:1foa.gif|left|200px]]<br /><applet load="1foa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1foa.gif|left|200px]]<br /><applet load="1foa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1foa, resolution 1.80&Aring;" />
 '''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''<br />
 ==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.
+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 Structure==
-FOA 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 MN, UD1 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOA OCA].
+FOA 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=MN:'>MN</scene>, <scene name='pdbligand=UD1:'>UD1</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1FOA OCA].
 ==Reference==
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 [[Category: Oryctolagus cuniculus]]
 [[Category: Single protein]]
-[[Category: Rini, J.M.]]
+[[Category: Rini, J M.]]
 [[Category: Sarkar, M.]]
 [[Category: Schachter, H.]]
-[[Category: Unligil, U.M.]]
+[[Category: Unligil, U M.]]
 [[Category: Yuwaraj, S.]]
 [[Category: Zhou, S.]]
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 [[Category: n-acetylglucosaminyltransferase i]]
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