4cn1 - Revision history

OCA at 12:12, 20 December 2023

OCA — Wed, 20 Dec 2023 12:12:53 GMT

←Older revision		Revision as of 12:12, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900078:alpha-maltose+1-phosphate'>PRD_900078</scene></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]] 2.55Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900078:alpha-maltose+1-phosphate'>PRD_900078</scene></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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [https://pdbe.org/4cn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [https://www.ebi.ac.uk/pdbsum/4cn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cn1 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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [https://pdbe.org/4cn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [https://www.ebi.ac.uk/pdbsum/4cn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cn1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GLGE1_STRCO GLGE1_STRCO]] Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.<ref>PMID:21914799</ref>	+	[https://www.uniprot.org/uniprot/GLGE1_STRCO GLGE1_STRCO] Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.<ref>PMID:21914799</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:22, 14 September 2022

OCA — Wed, 14 Sep 2022 07:22:55 GMT

←Older revision		Revision as of 07:22, 14 September 2022
Line 3:		Line 3:
	<StructureSection load='4cn1' size='340' side='right'caption='[[4cn1]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='4cn1' size='340' side='right'caption='[[4cn1]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces~~ coelicolor~~" (muller 1908) lieske 1921~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~M1F~~:ALPHA-~~MALTOSE+~~1-PHOSPHATE'>~~M1F~~</scene><~~/td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900078:alpha-maltose+1-phosphate'>PRD_900078</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td>~~<td class="sblockDat">[[4cn4\|4cn4]]~~, ~~[[4cn6\|4cn6]]~~<~~/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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [https://pdbe.org/4cn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [https://www.ebi.ac.uk/pdbsum/4cn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cn1 ProSAT]</span></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>[http://en.wikipedia.org/wiki/Starch_synthase_(maltosyl-transferring) Starch synthase (maltosyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.16 2.4.99.16] </~~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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [~~http~~://pdbe.org/4cn1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cn1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cn1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GLGE1_STRCO GLGE1_STRCO]] Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.<ref>PMID:21914799</ref>	+	[[https://www.uniprot.org/uniprot/GLGE1_STRCO GLGE1_STRCO]] Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.<ref>PMID:21914799</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bornemann, S]]	+	[[Category: Streptomyces coelicolor]]
-	[[Category: Lawson~~, D M~~]]	+	[[Category: Bornemann S]]
-	[[Category: Rashid~~, A M~~]]	+	[[Category: Lawson DM]]
-	[[Category: Saalbach, G]]	+	[[Category: Rashid AM]]
-	[[Category: Stevenson~~, C E.M~~]]	+	[[Category: Saalbach G]]
-	[[Category: Svergun~~, D I~~]]	+	[[Category: Stevenson CEM]]
-	[[Category: Syson, K]]	+	[[Category: Svergun DI]]
-	[[Category: Tang, M]]	+	[[Category: Syson K]]
-	[[Category: Tuukanen, A]]	+	[[Category: Tang M]]
-	[[Category: Withers~~, S G]]~~	+	[[Category: Tuukanen A]]
-	~~[[Category: Alpha-glucan biosynthesis]]~~	+	[[Category: Withers SG]]
-	~~[[Category: Drug target]]~~	+
-	~~[[Category: Glycoside hydrolase family 13_3]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 09:40, 20 March 2019

OCA — Wed, 20 Mar 2019 09:40:54 GMT

←Older revision		Revision as of 09:40, 20 March 2019
Line 1:		Line 1:

	==GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound==		==GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound==
-	<StructureSection load='4cn1' size='340' side='right' caption='[[4cn1]], [[Resolution\|resolution]] 2.55Å' scene=''>	+	<StructureSection load='4cn1' size='340' side='right'caption='[[4cn1]], [[Resolution\|resolution]] 2.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cn4\|4cn4]], [[4cn6\|4cn6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cn4\|4cn4]], [[4cn6\|4cn6]]</td></tr>
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Bornemann, S]]		[[Category: Bornemann, S]]
	[[Category: Lawson, D M]]		[[Category: Lawson, D M]]

OCA at 11:25, 5 August 2016

OCA — Fri, 05 Aug 2016 11:25:53 GMT

←Older revision		Revision as of 11:25, 5 August 2016
Line 1:		Line 1:
		+
	==GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound==		==GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound==
	<StructureSection load='4cn1' size='340' side='right' caption='[[4cn1]], [[Resolution\|resolution]] 2.55Å' scene=''>		<StructureSection load='4cn1' size='340' side='right' caption='[[4cn1]], [[Resolution\|resolution]] 2.55Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cn4\|4cn4]], [[4cn6\|4cn6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cn4\|4cn4]], [[4cn6\|4cn6]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Starch_synthase_(maltosyl-transferring) Starch synthase (maltosyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.16 2.4.99.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Starch_synthase_(maltosyl-transferring) Starch synthase (maltosyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.16 2.4.99.16] </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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://pdbe.org/4cn1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cn1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4cn1" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:00, 25 December 2014

OCA — Thu, 25 Dec 2014 02:00:38 GMT

←Older revision		Revision as of 02:00, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cn4\|4cn4]], [[4cn6\|4cn6]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cn4\|4cn4]], [[4cn6\|4cn6]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Starch_synthase_(maltosyl-transferring) Starch synthase (maltosyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.16 2.4.99.16] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Starch_synthase_(maltosyl-transferring) Starch synthase (maltosyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.16 2.4.99.16] </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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GLGE1_STRCO GLGE1_STRCO]] Maltosyltransferase that uses maltose 1-phosphate (M1P) as the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Maltooligosaccharides with a degree of polymerization (DP) superior or equal to 4 are efficient acceptors, with DP6 being optimal in the GlgE-catalyzed polymerization with M1P. Is specific for the alpha-anomer of M1P as substrate, since the beta-anomer of M1P gives no activity. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.<ref>PMID:21914799</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 16:
	Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds alpha-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate.,Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S Biochemistry. 2014 Apr 22;53(15):2494-504. doi: 10.1021/bi500183c. Epub 2014 Apr , 11. PMID:24689960<ref>PMID:24689960</ref>		Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds alpha-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate.,Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S Biochemistry. 2014 Apr 22;53(15):2494-504. doi: 10.1021/bi500183c. Epub 2014 Apr , 11. PMID:24689960<ref>PMID:24689960</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 20:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bornemann, S.]]	+	[[Category: Bornemann, S]]
-	[[Category: Lawson, D M.]]	+	[[Category: Lawson, D M]]
-	[[Category: Rashid, A M.]]	+	[[Category: Rashid, A M]]
-	[[Category: Saalbach, G.]]	+	[[Category: Saalbach, G]]
-	[[Category: Stevenson, C E.M.]]	+	[[Category: Stevenson, C E.M]]
-	[[Category: Svergun, D I.]]	+	[[Category: Svergun, D I]]
-	[[Category: Syson, K.]]	+	[[Category: Syson, K]]
-	[[Category: Tang, M.]]	+	[[Category: Tang, M]]
-	[[Category: Tuukanen, A.]]	+	[[Category: Tuukanen, A]]
-	[[Category: Withers, S G.]]	+	[[Category: Withers, S G]]
	[[Category: Alpha-glucan biosynthesis]]		[[Category: Alpha-glucan biosynthesis]]
	[[Category: Drug target]]		[[Category: Drug target]]
	[[Category: Glycoside hydrolase family 13_3]]		[[Category: Glycoside hydrolase family 13_3]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 09:09, 21 May 2014

OCA — Wed, 21 May 2014 09:09:40 GMT

←Older revision		Revision as of 09:09, 21 May 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound==
		+	<StructureSection load='4cn1' size='340' side='right' caption='[[4cn1]], [[Resolution\|resolution]] 2.55Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4cn4\|4cn4]], [[4cn6\|4cn6]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Starch_synthase_(maltosyl-transferring) Starch synthase (maltosyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.99.16 2.4.99.16] </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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	GlgE (EC 2.4.99.16) is an alpha-maltose 1-phosphate:(1-->4)-alpha-d-glucan 4-alpha-d-maltosyltransferase of the CAZy glycoside hydrolase 13_3 family. It is the defining enzyme of a bacterial alpha-glucan biosynthetic pathway and is a genetically validated anti-tuberculosis target. It catalyzes the alpha-retaining transfer of maltosyl units from alpha-maltose 1-phosphate to maltooligosaccharides and is predicted to use a double-displacement mechanism. Evidence of this mechanism was obtained using a combination of site-directed mutagenesis of Streptomyces coelicolor GlgE isoform I, substrate analogues, protein crystallography, and mass spectrometry. The X-ray structures of alpha-maltose 1-phosphate bound to a D394A mutein and a beta-2-deoxy-2-fluoromaltosyl-enzyme intermediate with a E423A mutein were determined. There are few examples of CAZy glycoside hydrolase family 13 members that have had their glycosyl-enzyme intermediate structures determined, and none before now have been obtained with a 2-deoxy-2-fluoro substrate analogue. The covalent modification of Asp394 was confirmed using mass spectrometry. A similar modification of wild-type GlgE proteins from S. coelicolor and Mycobacterium tuberculosis was also observed. Small-angle X-ray scattering of the M. tuberculosis enzyme revealed a homodimeric assembly similar to that of the S. coelicolor enzyme but with slightly differently oriented monomers. The deeper understanding of the structure-function relationships of S. coelicolor GlgE will aid the development of inhibitors of the M. tuberculosis enzyme.

-	~~The entry 4cn1 is ON HOLD until Paper Publication~~	+	Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds alpha-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate.,Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S Biochemistry. 2014 Apr 22;53(15):2494-504. doi: 10.1021/bi500183c. Epub 2014 Apr , 11. PMID:24689960<ref>PMID:24689960</ref>

-	~~Authors: Syson~~, K.~~, Stevenson, C~~.E.M., Rashid, A.M., Saalbach, G., ~~Tang,~~ M.~~, Tuukanen, A.,~~ Svergun, D.I., ~~Withers, S.G~~., ~~Lawson, D.~~M., ~~Bornemann~~, S.	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose~~-~~1-phosphate bound~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Bornemann, S.]]
		+	[[Category: Lawson, D M.]]
		+	[[Category: Rashid, A M.]]
		+	[[Category: Saalbach, G.]]
		+	[[Category: Stevenson, C E.M.]]
		+	[[Category: Svergun, D I.]]
		+	[[Category: Syson, K.]]
		+	[[Category: Tang, M.]]
		+	[[Category: Tuukanen, A.]]
		+	[[Category: Withers, S G.]]
		+	[[Category: Alpha-glucan biosynthesis]]
		+	[[Category: Drug target]]
		+	[[Category: Glycoside hydrolase family 13_3]]
		+	[[Category: Hydrolase]]

OCA: Protected "4cn1" [edit=sysop:move=sysop]

OCA — Wed, 29 Jan 2014 06:46:13 GMT

Protected "4cn1" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:46, 29 January 2014

OCA: New page: '''Unreleased structure''' The entry 4cn1 is ON HOLD until Paper Publication Authors: Syson, K., Stevenson, C.E.M., Rashid, A.M., Saalbach, G., Tang, M., Tuukanen, A., Svergun, D.I., Wi...

OCA — Wed, 29 Jan 2014 06:46:11 GMT

New page: '''Unreleased structure''' The entry 4cn1 is ON HOLD until Paper Publication Authors: Syson, K., Stevenson, C.E.M., Rashid, A.M., Saalbach, G., Tang, M., Tuukanen, A., Svergun, D.I., Wi...

New page

'''Unreleased structure'''

The entry 4cn1 is ON HOLD until Paper Publication

Authors: Syson, K., Stevenson, C.E.M., Rashid, A.M., Saalbach, G., Tang, M., Tuukanen, A., Svergun, D.I., Withers, S.G., Lawson, D.M., Bornemann, S.

Description: GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose-1-phosphate bound