3zt6
From Proteopedia
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==GLGE ISOFORM 1 FROM STREPTOMYCES COELICOLOR WITH ALPHA-CYCLODEXTRIN AND MALTOSE BOUND== | ==GLGE ISOFORM 1 FROM STREPTOMYCES COELICOLOR WITH ALPHA-CYCLODEXTRIN AND MALTOSE BOUND== | ||
<StructureSection load='3zt6' size='340' side='right' caption='[[3zt6]], [[Resolution|resolution]] 2.19Å' scene=''> | <StructureSection load='3zt6' size='340' side='right' caption='[[3zt6]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3zt6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3zt6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZT6 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACX:ALPHA-CYCLODEXTRIN+(CYCLOHEXA-AMYLOSE)'>ACX</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACX:ALPHA-CYCLODEXTRIN+(CYCLOHEXA-AMYLOSE)'>ACX</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zst|3zst]], [[3zss|3zss]], [[3zt7|3zt7]], [[3zt5|3zt5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zst|3zst]], [[3zss|3zss]], [[3zt7|3zt7]], [[3zt5|3zt5]]</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=3zt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zt6 RCSB], [http://www.ebi.ac.uk/pdbsum/3zt6 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=3zt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zt6 OCA], [http://pdbe.org/3zt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zt6 RCSB], [http://www.ebi.ac.uk/pdbsum/3zt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zt6 ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3zt6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Streptomyces coelicolor]] | ||
[[Category: Bornemann, S]] | [[Category: Bornemann, S]] | ||
[[Category: Bruton, C J]] | [[Category: Bruton, C J]] | ||
Revision as of 09:26, 11 August 2016
GLGE ISOFORM 1 FROM STREPTOMYCES COELICOLOR WITH ALPHA-CYCLODEXTRIN AND MALTOSE BOUND
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