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| | ==Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose== | | ==Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose== |
| - | <StructureSection load='4lq1' size='340' side='right' caption='[[4lq1]], [[Resolution|resolution]] 2.55Å' scene=''> | + | <StructureSection load='4lq1' size='340' side='right'caption='[[4lq1]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lq1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LQ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lq1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LQ1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1m7x|1m7x]], [[4lpc|4lpc]]</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=4lq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lq1 OCA], [https://pdbe.org/4lq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lq1 RCSB], [https://www.ebi.ac.uk/pdbsum/4lq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lq1 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glgB, b3432, JW3395 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,4-alpha-glucan_branching_enzyme 1,4-alpha-glucan branching enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.18 2.4.1.18] </span></td></tr>
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| - | <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=4lq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lq1 OCA], [http://pdbe.org/4lq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lq1 RCSB], [http://www.ebi.ac.uk/pdbsum/4lq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lq1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLGB_ECOLI GLGB_ECOLI]] Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position (By similarity). | + | [https://www.uniprot.org/uniprot/GLGB_ECOLI GLGB_ECOLI] Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: 1,4-alpha-glucan branching enzyme]] | + | [[Category: Large Structures]] |
| - | [[Category: Feng, L]] | + | [[Category: Feng L]] |
| - | [[Category: Geiger, J H]] | + | [[Category: Geiger JH]] |
| - | [[Category: Alpha/beta barrel]]
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| - | [[Category: Branching enzyme]]
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| - | [[Category: Linear polysaccharide]]
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| - | [[Category: Maltohexaose]]
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| - | [[Category: Starch biosynthetic pathway]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
GLGB_ECOLI Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position (By similarity).
Publication Abstract from PubMed
Branching enzyme is responsible for all branching of glycogen and starch. It is an unusual member of the alpha-amylase family because it has both alpha-1,4-amylase activity and alpha-1,6-transferase activity [Drummond, G. S., et al. (1972) Eur. J. Biochem. 26, 168-176]. It also does not react with shorter glucans, though it will bind much longer substrates and substrate mimics [Binderup, K., et al. (2002) Arch. Biochem. Biophys. 397, 279-285]. In an effort to better understand how branching enzyme interacts with its polymeric substrate, we have determined the structure of Delta112 Escherichia coli branching enzyme bound to maltoheptaose and maltohexaose. Together, these structures define six distinct oligosaccharide binding sites on the surface of E. coli branching enzyme. Most of these binding sites surround the edge of the beta-barrel domain and are quite far from the active site. Surprisingly, there is no evidence of oligosaccharide binding in the active site of the enzyme. The closest bound oligosaccharide resides almost 18 A from the active site. Mutations to conserved residues in binding sites I and VI had a debilitating effect on the activity of the enzyme.
Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides.,Feng L, Fawaz R, Hovde S, Gilbert L, Chiou J, Geiger JH Biochemistry. 2015 Sep 25. PMID:26280198[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feng L, Fawaz R, Hovde S, Gilbert L, Chiou J, Geiger JH. Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides. Biochemistry. 2015 Sep 25. PMID:26280198 doi:http://dx.doi.org/10.1021/acs.biochem.5b00228
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