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<StructureSection load='3zss' size='340' side='right'caption='[[3zss]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3zss' size='340' side='right'caption='[[3zss]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3zss]] is a 4 chain structure with sequence from [https://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=3ZSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZSS FirstGlance]. <br>
<table><tr><td colspan='2'>[[3zss]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZSS FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zst|3zst]], [[3zt7|3zt7]], [[3zt6|3zt6]], [[3zt5|3zt5]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=3zss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zss OCA], [https://pdbe.org/3zss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zss RCSB], [https://www.ebi.ac.uk/pdbsum/3zss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zss ProSAT]</span></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=3zss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zss OCA], [https://pdbe.org/3zss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zss RCSB], [https://www.ebi.ac.uk/pdbsum/3zss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zss ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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>
[https://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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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bornemann, S]]
[[Category: Streptomyces coelicolor]]
[[Category: Bruton, C J]]
[[Category: Bornemann S]]
[[Category: Chater, K F]]
[[Category: Bruton CJ]]
[[Category: Fairhurst, S A]]
[[Category: Chater KF]]
[[Category: Field, R A]]
[[Category: Fairhurst SA]]
[[Category: Lawson, D M]]
[[Category: Field RA]]
[[Category: Nair, A]]
[[Category: Lawson DM]]
[[Category: Rejzek, M]]
[[Category: Nair A]]
[[Category: Stevenson, C E.M]]
[[Category: Rejzek M]]
[[Category: Syson, K]]
[[Category: Stevenson CEM]]
[[Category: Alpha-glucan biosynthesis]]
[[Category: Syson K]]
[[Category: Glycoside hydrolase family 13_3]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/3zss"