This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3zo9

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 17:04, 4 August 2016

The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis

Structural highlights

3zo9 is a 2 chain structure with sequence from Mycobacterium smegmatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	3zoa
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zo9"

@@ Line 1: / Line 1: @@
 ==The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis==
 <StructureSection load='3zo9' size='340' side='right' caption='[[3zo9]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[3zoa|3zoa]]</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=3zo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zo9 RCSB], [http://www.ebi.ac.uk/pdbsum/3zo9 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=3zo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zo9 OCA], [http://pdbe.org/3zo9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zo9 RCSB], [http://www.ebi.ac.uk/pdbsum/3zo9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zo9 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3zo9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3zo9

From Proteopedia

Revision as of 17:04, 4 August 2016

The structure of Trehalose Synthase (TreS) of Mycobacterium smegmatis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox