4u2z
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==X-ray crystal structure of an Sco GlgEI-V279S/1,2,2-trifluromaltose complex== |
| - | + | <StructureSection load='4u2z' size='340' side='right' caption='[[4u2z]], [[Resolution|resolution]] 2.26Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4u2z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U2Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U2Z FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMO:2-DEOXY-2,2-DIFLUORO-4-O-ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-ARABINO-HEXOPYRANOSYL+FLUORIDE'>FMO</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u2y|4u2y]], [[4u31|4u31]], [[4u33|4u33]], [[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=4u2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u2z RCSB], [http://www.ebi.ac.uk/pdbsum/4u2z PDBsum]</span></td></tr> |
| - | [[Category: Ronning, D | + | </table> |
| - | [[Category: | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/GLGE1_STRCO GLGE1_STRCO]] 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 DP6 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. Alpha-D-glucose 1-phosphate cannot serve as a donor substrate, but alpha-maltosyl fluoride is an efficient donor in vitro. Exhibits an alpha-retaining catalytic mechanism, with evidence that maltooligosaccharide acceptors are extended at their non-reducing ends. Is also able to catalyze the reverse reaction in vitro, releasing M1P from glycogen or maltoheptaose in the presence of inorganic phosphate. Also catalyzes disproportionation reactions through maltosyl transfer between maltooligosaccharides. Is probably involved in a branched alpha-glucan biosynthetic pathway from trehalose, together with TreS, Mak and GlgB.<ref>PMID:21914799</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lindenberger, J J]] | ||
| + | [[Category: Ronning, D R]] | ||
| + | [[Category: Inhibitor complex fluorosugar maltosyl transferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 14:15, 22 July 2015
X-ray crystal structure of an Sco GlgEI-V279S/1,2,2-trifluromaltose complex
| |||||||||||
