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| | ==Crystal structure of M. tuberculosis TreS== | | ==Crystal structure of M. tuberculosis TreS== |
| - | <StructureSection load='4lxf' size='340' side='right' caption='[[4lxf]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4lxf' size='340' side='right'caption='[[4lxf]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lxf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LXF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lxf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LXF FirstGlance]. <br> |
| - | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0126, RVBD_0126 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=4lxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxf OCA], [https://pdbe.org/4lxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lxf RCSB], [https://www.ebi.ac.uk/pdbsum/4lxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxf 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/Maltose_alpha-D-glucosyltransferase Maltose alpha-D-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.16 5.4.99.16] </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=4lxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxf OCA], [http://pdbe.org/4lxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lxf RCSB], [http://www.ebi.ac.uk/pdbsum/4lxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Maltose alpha-D-glucosyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Besra, G S]] | + | [[Category: Besra GS]] |
| - | [[Category: Futterer, K]] | + | [[Category: Futterer K]] |
| - | [[Category: Roy, R]] | + | [[Category: Roy R]] |
| - | [[Category: Amylase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Maltose]]
| + | |
| - | [[Category: Trehalose]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Recent evidence established that the cell envelope of Mycobacterium tuberculosis, the bacillus causing tuberculosis (TB), is coated by an alpha-glucan-containing capsule that has been implicated in persistence in a mouse infection model. As one of three known metabolic routes to alpha-glucan in mycobacteria, the cytoplasmic GlgE-pathway converts trehalose to alpha(1 --> 4),alpha(1 --> 6)-linked glucan in 4 steps. Whether individual reaction steps, catalyzed by trehalose synthase TreS, maltokinase Pep2, and glycosyltransferases GlgE and GlgB, occur independently or in a coordinated fashion is not known. Here, we report the crystal structure of M. tuberculosis TreS, and show by small-angle X-ray scattering and analytical ultracentrifugation that TreS forms tetramers in solution. Together with Pep2, TreS forms a hetero-octameric complex, and we demonstrate that complex formation markedly accelerates maltokinase activity of Pep2. Thus, complex formation may act as part of a regulatory mechanism of the GlgE pathway, which overall must avoid accumulation of toxic pathway intermediates, such as maltose-1-phosphate, and optimize the use of scarce nutrients.
Synthesis of alpha-Glucan in Mycobacteria Involves a Hetero-octameric Complex of Trehalose Synthase TreS and Maltokinase Pep2.,Roy R, Usha V, Kermani A, Scott DJ, Hyde EI, Besra GS, Alderwick LJ, Futterer K ACS Chem Biol. 2013 Aug 13. PMID:23901909[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roy R, Usha V, Kermani A, Scott DJ, Hyde EI, Besra GS, Alderwick LJ, Futterer K. Synthesis of alpha-Glucan in Mycobacteria Involves a Hetero-octameric Complex of Trehalose Synthase TreS and Maltokinase Pep2. ACS Chem Biol. 2013 Aug 13. PMID:23901909 doi:10.1021/cb400508k
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