1fo9 - Revision history

OCA at 11:14, 27 March 2024

2024-03-27T11:14:49Z

←Older revision		Revision as of 11:14, 27 March 2024
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	<StructureSection load='1fo9' size='340' side='right'caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1fo9' size='340' side='right'caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~European_rabbit European rabbit~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1fo8\|1fo8]]~~, [[~~1foa~~\|~~1foa~~]]~~</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.5Å</td></tr>
-	~~<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://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 [https://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.101 2.4.1.101] </span>~~</td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [https://pdbe.org/1fo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fo9 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [https://pdbe.org/1fo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fo9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/MGAT1_RABIT MGAT1_RABIT]] Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.	+	[https://www.uniprot.org/uniprot/MGAT1_RABIT MGAT1_RABIT] Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fo9 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fo9 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	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.
-
-	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<ref>PMID:11032794</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1fo9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[O-GlcNAc transferase 3D structures\|O-GlcNAc transferase 3D structures]]		*[[O-GlcNAc transferase 3D structures\|O-GlcNAc transferase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]]
-	[[Category: European rabbit]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Rini~~, J M~~]]	+	[[Category: Oryctolagus cuniculus]]
-	[[Category: Sarkar, M]]	+	[[Category: Rini JM]]
-	[[Category: Schachter, H]]	+	[[Category: Sarkar M]]
-	[[Category: Unligil~~, U M~~]]	+	[[Category: Schachter H]]
-	[[Category: Yuwaraj, S]]	+	[[Category: Unligil UM]]
-	[[Category: Zhou, S]]	+	[[Category: Yuwaraj S]]
-	~~[[Category: 2-n-acetylglucosaminyltransferase]]~~	+	[[Category: Zhou S]]
-	~~[[Category: 3-mannosyl-glycoprotein beta-1]]~~	+
-	~~[[Category: Alpha-1]]~~	+
-	~~[[Category: Apo structure]]~~	+
-	~~[[Category: N-acetylglucosaminyltransferase i]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 11:12, 28 July 2021

2021-07-28T11:12:26Z

←Older revision		Revision as of 11:12, 28 July 2021
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	<StructureSection load='1fo9' size='340' side='right'caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1fo9' size='340' side='right'caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fo8\|1fo8]], [[1foa\|1foa]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://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 [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.101 2.4.1.101] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [~~http~~://pdbe.org/1fo9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1fo9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1fo9 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [https://pdbe.org/1fo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fo9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/MGAT1_RABIT MGAT1_RABIT]] Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.	+	[[https://www.uniprot.org/uniprot/MGAT1_RABIT MGAT1_RABIT]] Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[O-GlcNAc transferase\|O-GlcNAc transferase]]	+	*[[O-GlcNAc transferase 3D structures\|O-GlcNAc transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:37, 23 October 2019

2019-10-23T08:37:49Z

←Older revision

Revision as of 08:37, 23 October 2019

OCA at 09:27, 27 December 2017

2017-12-27T09:27:44Z

←Older revision		Revision as of 09:27, 27 December 2017
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		+
	==CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I==		==CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I==
	<StructureSection load='1fo9' size='340' side='right' caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1fo9' size='340' side='right' caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://pdbe.org/1fo9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://pdbe.org/1fo9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fo9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fo9_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fo9_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	</div>		</div>
	<div class="pdbe-citations 1fo9" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1fo9" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[O-GlcNAc transferase\|O-GlcNAc transferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:31, 9 February 2016

2016-02-09T07:31:17Z

←Older revision		Revision as of 07:31, 9 February 2016
Line 17:		Line 17:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fo9 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:00, 10 September 2015

2015-09-10T20:00:11Z

←Older revision		Revision as of 20:00, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1fo9' size='340' side='right' caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='1fo9' size='340' side='right' caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with 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=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://pdbe.org/1fo9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1fo9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]]		[[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]]
-	[[Category: ~~Oryctolagus cuniculus~~]]	+	[[Category: European rabbit]]
	[[Category: Rini, J M]]		[[Category: Rini, J M]]
	[[Category: Sarkar, M]]		[[Category: Sarkar, M]]

OCA at 05:23, 25 December 2014

2014-12-25T05:23:02Z

←Older revision		Revision as of 05:23, 25 December 2014
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	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MGAT1_RABIT MGAT1_RABIT]] Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:44, 22 December 2014

2014-12-22T22:44:13Z

←Older revision		Revision as of 22:44, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with 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=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with 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=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 34:
	[[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]]
-	[[Category: Rini, J M.]]	+	[[Category: Rini, J M]]
-	[[Category: Sarkar, M.]]	+	[[Category: Sarkar, M]]
-	[[Category: Schachter, H.]]	+	[[Category: Schachter, H]]
-	[[Category: Unligil, U M.]]	+	[[Category: Unligil, U M]]
-	[[Category: Yuwaraj, S.]]	+	[[Category: Yuwaraj, S]]
-	[[Category: Zhou, S.]]	+	[[Category: Zhou, S]]
	[[Category: 2-n-acetylglucosaminyltransferase]]		[[Category: 2-n-acetylglucosaminyltransferase]]
	[[Category: 3-mannosyl-glycoprotein beta-1]]		[[Category: 3-mannosyl-glycoprotein beta-1]]

OCA at 12:31, 28 September 2014

2014-09-28T12:31:08Z

←Older revision		Revision as of 12:31, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1fo9.~~png~~\|~~left~~\|200px]]	+	==CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I==
		+	<StructureSection load='1fo9' size='340' side='right' caption='[[1fo9]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1fo9]] is a 1 chain structure with 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=1FO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FO9 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fo8\|1fo8]], [[1foa\|1foa]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fo9 RCSB], [http://www.ebi.ac.uk/pdbsum/1fo9 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/1fo9_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.

-	~~{{STRUCTURE_1fo9\| PDB=1fo9 \| SCENE= }}~~	+	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<ref>PMID:11032794</ref>

-	~~===CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11032794}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1fo9]] is~~ a ~~1 chain structure with 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=1FO9 OCA].~~	+

	==See Also==		==See Also==
	*[[O-GlcNAc transferase\|O-GlcNAc transferase]]		*[[O-GlcNAc transferase\|O-GlcNAc transferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011032794<~~/~~ref~~><~~ref group="xtra">PMID:011467936</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[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]]

OCA at 13:07, 20 October 2012

2012-10-20T13:07:31Z

←Older revision		Revision as of 13:07, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1fo9]] is a 1 chain structure ~~of [[O-GlcNAc transferase]]~~ with 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=1FO9 OCA].	+	[[1fo9]] is a 1 chain structure with 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=1FO9 OCA].

	==See Also==		==See Also==