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| | <StructureSection load='3zo9' size='340' side='right'caption='[[3zo9]], [[Resolution|resolution]] 1.84Å' scene=''> | | <StructureSection load='3zo9' size='340' side='right'caption='[[3zo9]], [[Resolution|resolution]] 1.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zo9]] 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=3ZO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZO9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zo9]] 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=3ZO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZO9 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=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]] 1.84Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zoa|3zoa]]</div></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=MG:MAGNESIUM+ION'>MG</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=3zo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo9 OCA], [https://pdbe.org/3zo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zo9 RCSB], [https://www.ebi.ac.uk/pdbsum/3zo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zo9 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=3zo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo9 OCA], [https://pdbe.org/3zo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zo9 RCSB], [https://www.ebi.ac.uk/pdbsum/3zo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zo9 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 == |
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| | </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]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
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.
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pan YT, Koroth Edavana V, Jourdian WJ, Edmondson R, Carroll JD, Pastuszak I, Elbein AD. Trehalose synthase of Mycobacterium smegmatis: purification, cloning, expression, and properties of the enzyme. Eur J Biochem. 2004 Nov;271(21):4259-69. PMID:15511231 doi:10.1111/j.1432-1033.2004.04365.x
- ↑ Pan YT, Carroll JD, Asano N, Pastuszak I, Edavana VK, Elbein AD. Trehalose synthase converts glycogen to trehalose. FEBS J. 2008 Jul;275(13):3408-20. doi: 10.1111/j.1742-4658.2008.06491.x. Epub, 2008 May 23. PMID:18505459 doi:10.1111/j.1742-4658.2008.06491.x
- ↑ Elbein AD, Pastuszak I, Tackett AJ, Wilson T, Pan YT. The last step in the conversion of trehalose to glycogen:A mycobacterial enzyme that transfers maltose from maltose-1-phosphate to glycogen. J Biol Chem. 2010 Jan 29. PMID:20118231 doi:M109.033944
- ↑ Zhang R, Pan YT, He S, Lam M, Brayer GD, Elbein AD, Withers SG. Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis. J Biol Chem. 2011 Oct 14;286(41):35601-9. doi: 10.1074/jbc.M111.280362. Epub 2011, Aug 12. PMID:21840994 doi:10.1074/jbc.M111.280362
- ↑ Caner S, Nguyen N, Aguda A, Zhang R, Pan YT, Withers SG, Brayer GD. The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode. Glycobiology. 2013 Jul 5. PMID:23735230 doi:10.1093/glycob/cwt044
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