4u33
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Structure of Mtb GlgE bound to maltose== |
| - | + | <StructureSection load='4u33' size='340' side='right' caption='[[4u33]], [[Resolution|resolution]] 3.29Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4u33]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U33 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u2y|4u2y]], [[4u2z|4u2z]], [[4u31|4u31]], [[4u3c|4u3c]]</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> | |
| - | [[Category: | + | <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=4u33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u33 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u33 RCSB], [http://www.ebi.ac.uk/pdbsum/4u33 PDBsum]</span></td></tr> |
| - | [[Category: Ronning, D | + | </table> |
| - | [[Category: | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/GLGE_MYCTO GLGE_MYCTO]] Essential 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 DP5 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. Exhibits an alpha-retaining catalytic mechanism. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB (By similarity). | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lindenberger, J J]] | ||
| + | [[Category: Ronning, D R]] | ||
| + | [[Category: Complex wild-type maltose maltosyl-transferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 14:15, 22 July 2015
Structure of Mtb GlgE bound to maltose
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