4cn1
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4cn1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CN1 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1F:ALPHA-MALTOSE+1-PHOSPHATE'>M1F</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cn4|4cn4]], [[4cn6|4cn6]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cn4|4cn4]], [[4cn6|4cn6]]</td></tr> |
| - | <tr><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> | + | <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> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 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=4cn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cn1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cn1 RCSB], [http://www.ebi.ac.uk/pdbsum/4cn1 PDBsum]</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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Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds alpha-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate.,Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S Biochemistry. 2014 Apr 22;53(15):2494-504. doi: 10.1021/bi500183c. Epub 2014 Apr , 11. PMID:24689960<ref>PMID:24689960</ref> | Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds alpha-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate.,Syson K, Stevenson CE, Rashid AM, Saalbach G, Tang M, Tuukkanen A, Svergun DI, Withers SG, Lawson DM, Bornemann S Biochemistry. 2014 Apr 22;53(15):2494-504. doi: 10.1021/bi500183c. Epub 2014 Apr , 11. PMID:24689960<ref>PMID:24689960</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Bornemann, S | + | [[Category: Bornemann, S]] |
| - | [[Category: Lawson, D M | + | [[Category: Lawson, D M]] |
| - | [[Category: Rashid, A M | + | [[Category: Rashid, A M]] |
| - | [[Category: Saalbach, G | + | [[Category: Saalbach, G]] |
| - | [[Category: Stevenson, C E.M | + | [[Category: Stevenson, C E.M]] |
| - | [[Category: Svergun, D I | + | [[Category: Svergun, D I]] |
| - | [[Category: Syson, K | + | [[Category: Syson, K]] |
| - | [[Category: Tang, M | + | [[Category: Tang, M]] |
| - | [[Category: Tuukanen, A | + | [[Category: Tuukanen, A]] |
| - | [[Category: Withers, S G | + | [[Category: Withers, S G]] |
[[Category: Alpha-glucan biosynthesis]] | [[Category: Alpha-glucan biosynthesis]] | ||
[[Category: Drug target]] | [[Category: Drug target]] | ||
[[Category: Glycoside hydrolase family 13_3]] | [[Category: Glycoside hydrolase family 13_3]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 02:00, 25 December 2014
GlgE isoform 1 from Streptomyces coelicolor D394A mutant with maltose- 1-phosphate bound
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