1foa
From Proteopedia
(New page: 200px<br /><applet load="1foa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1foa, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1foa.gif|left|200px]]<br /><applet load="1foa" size=" | + | [[Image:1foa.gif|left|200px]]<br /><applet load="1foa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1foa, resolution 1.80Å" /> | caption="1foa, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''<br /> | '''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''<br /> | ||
==Overview== | ==Overview== | ||
| - | N:-acetylglucosaminyltransferase I (GnT I) serves as the gateway from | + | 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== | ==About this Structure== | ||
| - | 1FOA 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:// | + | 1FOA 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== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Rini, J | + | [[Category: Rini, J M.]] |
[[Category: Sarkar, M.]] | [[Category: Sarkar, M.]] | ||
[[Category: Schachter, H.]] | [[Category: Schachter, H.]] | ||
| - | [[Category: Unligil, U | + | [[Category: Unligil, U M.]] |
[[Category: Yuwaraj, S.]] | [[Category: Yuwaraj, S.]] | ||
[[Category: Zhou, S.]] | [[Category: Zhou, S.]] | ||
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[[Category: n-acetylglucosaminyltransferase i]] | [[Category: n-acetylglucosaminyltransferase i]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:48 2008'' |
Revision as of 10:40, 21 February 2008
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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.
About 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.
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:11032794
Page seeded by OCA on Thu Feb 21 12:40:48 2008
Categories: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase | Oryctolagus cuniculus | Single protein | Rini, J M. | Sarkar, M. | Schachter, H. | Unligil, U M. | Yuwaraj, S. | Zhou, S. | GOL | MN | UD1 | 2-n-acetylglucosaminyltransferase | 3-mannosyl-glycoprotein | Alpha-1 | Beta-1 | Donor substrate and metal ion complex | N-acetylglucosaminyltransferase i
