3zoa - Revision history

OCA at 11:08, 20 December 2023

OCA — Wed, 20 Dec 2023 11:08:09 GMT

←Older revision		Revision as of 11:08, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='3zoa' size='340' side='right'caption='[[3zoa]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='3zoa' size='340' side='right'caption='[[3zoa]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zoa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Mycobacterium_smegmatis Mycobacterium~~ smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zoa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOA FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA~~-~~D-GLUCOSE'>GLC</scene>~~, ~~<scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.85Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene><~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRD_900007:alpha-acarbose'>PRD_900007</scene></td></tr>
-	<~~tr id~~='~~related~~'><~~td class="sblockLbl"~~><~~b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"~~><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[3zo9\|3zo9]]~~</~~div~~></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=3zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoa OCA], [https://pdbe.org/3zoa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zoa RCSB], [https://www.ebi.ac.uk/pdbsum/3zoa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zoa 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=3zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoa OCA], [https://pdbe.org/3zoa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zoa RCSB], [https://www.ebi.ac.uk/pdbsum/3zoa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zoa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TRES_MYCS2 TRES_MYCS2]] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.<ref>PMID:15511231</ref> <ref>PMID:18505459</ref> <ref>PMID:20118231</ref> <ref>PMID:21840994</ref>	+	[https://www.uniprot.org/uniprot/TRES_MYCS2 TRES_MYCS2] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.<ref>PMID:15511231</ref> <ref>PMID:18505459</ref> <ref>PMID:20118231</ref> <ref>PMID:21840994</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Mycobacterium~~ smegmatis]]	+	[[Category: Mycolicibacterium smegmatis]]
-	[[Category: Aguda, A]]	+	[[Category: Aguda A]]
-	[[Category: Brayer~~, G D~~]]	+	[[Category: Brayer GD]]
-	[[Category: Caner, S]]	+	[[Category: Caner S]]
-	[[Category: Nguyen, N]]	+	[[Category: Nguyen N]]
-	[[Category: Pan~~, Y T~~]]	+	[[Category: Pan YT]]
-	[[Category: Withers~~, S G~~]]	+	[[Category: Withers SG]]
-	[[Category: Zhang, R]]	+	[[Category: Zhang R]]
-	~~[[Category: Drug design]]~~	+
-	~~[[Category: Glycohydrolase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Tuberculosis~~]]	+

OCA at 07:04, 18 August 2022

OCA — Thu, 18 Aug 2022 07:04:57 GMT

←Older revision		Revision as of 07:04, 18 August 2022
Line 1:		Line 1:

	==The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose==		==The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose==
-	<StructureSection load='3zoa' size='340' side='right' caption='[[3zoa]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='3zoa' size='340' side='right'caption='[[3zoa]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zoa]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3ZOA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zoa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~ACR~~:~~ALPHA-ACARBOSE~~'>~~ACR~~</scene>, <scene name='pdbligand=CA:~~CALCIUM~~+ION'>CA</scene>, <scene name='pdbligand=CL:~~CHLORIDE+ION~~'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zo9\|3zo9]]</td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene></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=3zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoa OCA], [~~http~~://pdbe.org/3zoa PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3zoa RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3zoa PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3zoa ProSAT]</span></td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zo9\|3zo9]]</div></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=3zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoa OCA], [https://pdbe.org/3zoa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zoa RCSB], [https://www.ebi.ac.uk/pdbsum/3zoa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zoa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TRES_MYCS2 TRES_MYCS2]] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.<ref>PMID:15511231</ref> <ref>PMID:18505459</ref> <ref>PMID:20118231</ref> <ref>PMID:21840994</ref>	+	[[https://www.uniprot.org/uniprot/TRES_MYCS2 TRES_MYCS2]] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.<ref>PMID:15511231</ref> <ref>PMID:18505459</ref> <ref>PMID:20118231</ref> <ref>PMID:21840994</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Mycobacterium smegmatis]]		[[Category: Mycobacterium smegmatis]]
	[[Category: Aguda, A]]		[[Category: Aguda, A]]

OCA at 18:52, 5 August 2016

OCA — Fri, 05 Aug 2016 18:52:18 GMT

←Older revision		Revision as of 18:52, 5 August 2016
Line 1:		Line 1:
		+
	==The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose==		==The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose==
	<StructureSection load='3zoa' size='340' side='right' caption='[[3zoa]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='3zoa' size='340' side='right' caption='[[3zoa]], [[Resolution\|resolution]] 1.85Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACR:ALPHA-ACARBOSE'>ACR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACR:ALPHA-ACARBOSE'>ACR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zo9\|3zo9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zo9\|3zo9]]</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=3zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zoa RCSB], [http://www.ebi.ac.uk/pdbsum/3zoa 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=3zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoa OCA], [http://pdbe.org/3zoa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zoa RCSB], [http://www.ebi.ac.uk/pdbsum/3zoa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zoa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 3zoa" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:07, 25 December 2014

OCA — Thu, 25 Dec 2014 21:07:24 GMT

←Older revision		Revision as of 21:07, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3zoa\| PDB=3zoa \| SCENE= }}~~	+	==The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose==
-	===The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose===	+	<StructureSection load='3zoa' size='340' side='right' caption='[[3zoa]], [[Resolution\|resolution]] 1.85Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23735230}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3zoa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZOA FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACR:ALPHA-ACARBOSE'>ACR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zo9\|3zo9]]</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=3zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zoa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zoa RCSB], [http://www.ebi.ac.uk/pdbsum/3zoa PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/TRES_MYCS2 TRES_MYCS2]] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.<ref>PMID:15511231</ref> <ref>PMID:18505459</ref> <ref>PMID:20118231</ref> <ref>PMID:21840994</ref>		[[http://www.uniprot.org/uniprot/TRES_MYCS2 TRES_MYCS2]] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.<ref>PMID:15511231</ref> <ref>PMID:18505459</ref> <ref>PMID:20118231</ref> <ref>PMID:21840994</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Trehalose synthase (TreS) catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide. Given the importance of trehalose to survival of mycobacteria, there has been considerable interest in understanding the enzymes involved in its production; indeed the structures of the key enzymes in the other two pathways have already been determined. Herein, we present the first structure of TreS from Mycobacterium smegmatis, thereby providing insights into the catalytic machinery involved in this intriguing intramolecular reaction. This structure, which is of interest both mechanistically and as a potential pharmaceutical target, reveals a narrow and enclosed active site pocket within which intramolecular substrate rearrangements can occur. We also present the structure of a complex of TreS with acarbose, revealing a hitherto unsuspected oligosaccharide-binding site within the C-terminal domain. This may well provide an anchor point for the association of TreS with glycogen, thereby enhancing its role in glycogen biosynthesis and degradation.

-	~~==About this Structure==~~	+	The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode.,Caner S, Nguyen N, Aguda A, Zhang R, Pan YT, Withers SG, Brayer GD Glycobiology. 2013 Jul 5. PMID:23735230<ref>PMID:23735230</ref>
-	~~[[3zoa]] is a 2 chain~~ structure ~~with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis~~ Mycobacterium smegmatis]. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=3ZOA OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:023735230</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Mycobacterium smegmatis]]		[[Category: Mycobacterium smegmatis]]
-	[[Category: Aguda, A.]]	+	[[Category: Aguda, A]]
-	[[Category: Brayer, G D.]]	+	[[Category: Brayer, G D]]
-	[[Category: Caner, S.]]	+	[[Category: Caner, S]]
-	[[Category: Nguyen, N.]]	+	[[Category: Nguyen, N]]
-	[[Category: Pan, Y T.]]	+	[[Category: Pan, Y T]]
-	[[Category: Withers, S G.]]	+	[[Category: Withers, S G]]
-	[[Category: Zhang, R.]]	+	[[Category: Zhang, R]]
	[[Category: Drug design]]		[[Category: Drug design]]
	[[Category: Glycohydrolase]]		[[Category: Glycohydrolase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Tuberculosis]]		[[Category: Tuberculosis]]

OCA at 04:53, 18 July 2013

OCA — Thu, 18 Jul 2013 04:53:48 GMT

←Older revision		Revision as of 04:53, 18 July 2013
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-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_3zoa\| PDB=3zoa \| SCENE= }}
		+	===The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis in complex with acarbose===
		+	{{ABSTRACT_PUBMED_23735230}}

-	~~The entry 3zoa~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/TRES_MYCS2 TRES_MYCS2]] Catalyzes the reversible interconversion of maltose and trehalose by transglucosylation. Maltose is the preferred substrate. To a lesser extent, also displays amylase activity, catalyzing the endohydrolysis of (1->4)-alpha-D-glucosidic linkages in glycogen and maltooligosaccharides such as maltoheptaose, to produce maltose which then can be converted to trehalose. TreS plays a key role in the utilization of trehalose for the production of glycogen, and might also function as a sensor and/or regulator of trehalose levels within the cell. Thus, when trehalose levels in the cell become dangerously low, TreS can expedite the conversion of glycogen to maltose via its amylase activity and then convert the maltose to trehalose; but this enzyme also can expedite or promote the conversion of trehalose to glycogen when cytoplasmic trehalose levels become too high. Is also able to catalyze the hydrolytic cleavage of alpha-aryl glucosides, as well as alpha-glucosyl fluoride in vitro.<ref>PMID:15511231</ref> <ref>PMID:18505459</ref> <ref>PMID:20118231</ref> <ref>PMID:21840994</ref>

-	~~Authors~~: ~~Caner, S~~.~~, Nguyen, N~~.~~, Aguda, A~~.~~, Zhang, R., Pan, Y.T., Withers, S~~.G.~~, Brayer, G~~.D.	+	==About this Structure==
		+	[[3zoa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOA OCA].

-	~~Description~~: ~~Novel Active Site and Inhibition Sites Identified in Trehalose Synthase~~	+	==Reference==
		+	<ref group="xtra">PMID:023735230</ref><references group="xtra"/><references/>
		+	[[Category: Mycobacterium smegmatis]]
		+	[[Category: Aguda, A.]]
		+	[[Category: Brayer, G D.]]
		+	[[Category: Caner, S.]]
		+	[[Category: Nguyen, N.]]
		+	[[Category: Pan, Y T.]]
		+	[[Category: Withers, S G.]]
		+	[[Category: Zhang, R.]]
		+	[[Category: Drug design]]
		+	[[Category: Glycohydrolase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Tuberculosis]]

OCA at 13:35, 6 March 2013

OCA — Wed, 06 Mar 2013 13:35:23 GMT

←Older revision		Revision as of 13:35, 6 March 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3zoa is ON HOLD	+	The entry 3zoa is ON HOLD until Paper Publication

	Authors: Caner, S., Nguyen, N., Aguda, A., Zhang, R., Pan, Y.T., Withers, S.G., Brayer, G.D.		Authors: Caner, S., Nguyen, N., Aguda, A., Zhang, R., Pan, Y.T., Withers, S.G., Brayer, G.D.

	Description: Novel Active Site and Inhibition Sites Identified in Trehalose Synthase		Description: Novel Active Site and Inhibition Sites Identified in Trehalose Synthase

OCA: Protected "3zoa" [edit=sysop:move=sysop]

OCA — Wed, 27 Feb 2013 14:07:46 GMT

Protected "3zoa" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:07, 27 February 2013

OCA: New page: '''Unreleased structure''' The entry 3zoa is ON HOLD Authors: Caner, S., Nguyen, N., Aguda, A., Zhang, R., Pan, Y.T., Withers, S.G., Brayer, G.D. Description: Novel Active Site and Inh...

OCA — Wed, 27 Feb 2013 14:07:45 GMT

New page: '''Unreleased structure''' The entry 3zoa is ON HOLD Authors: Caner, S., Nguyen, N., Aguda, A., Zhang, R., Pan, Y.T., Withers, S.G., Brayer, G.D. Description: Novel Active Site and Inh...

New page

'''Unreleased structure'''

The entry 3zoa is ON HOLD

Authors: Caner, S., Nguyen, N., Aguda, A., Zhang, R., Pan, Y.T., Withers, S.G., Brayer, G.D.

Description: Novel Active Site and Inhibition Sites Identified in Trehalose Synthase