3vu2

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<StructureSection load='3vu2' size='340' side='right'caption='[[3vu2]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
<StructureSection load='3vu2' size='340' side='right'caption='[[3vu2]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_rice Japanese rice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VU2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vu2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VU2 FirstGlance]. <br>
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</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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3amk|3amk]]</div></td></tr>
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<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_900030:alpha-maltopentaose'>PRD_900030</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SBE1, RBE1, Os06g0726400, LOC_Os06g51084, P0017G10.8-1, P0017G10.8-2, P0548E04.28-1, P0548E04.28-2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Japanese rice])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1,4-alpha-glucan_branching_enzyme 1,4-alpha-glucan branching enzyme], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3vu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vu2 OCA], [https://pdbe.org/3vu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vu2 RCSB], [https://www.ebi.ac.uk/pdbsum/3vu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vu2 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=3vu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vu2 OCA], [https://pdbe.org/3vu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vu2 RCSB], [https://www.ebi.ac.uk/pdbsum/3vu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vu2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GLGB_ORYSJ GLGB_ORYSJ]] Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch 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.
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[https://www.uniprot.org/uniprot/GLGB_ORYSJ GLGB_ORYSJ] Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch 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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Starch branching enzyme (SBE) catalyzes the cleavage of alpha-1,4-linkages and the subsequent transfer of alpha-1,4 glucan to form an alpha-1,6 branch point in amylopectin. We determined the crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose at a resolution of 2.2A. Maltopentaose bound to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48 (CBM48), and alpha-amylase domain. In addition, glucose moieties could be observed at molecular surfaces on the N-terminal helix (alpha2) and CBM48. Amino acid residues involved in the carbohydrate bindings are highly conserved in other SBEs, suggesting their generally conserved role in substrate binding for SBEs.
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Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose.,Chaen K, Noguchi J, Omori T, Kakuta Y, Kimura M Biochem Biophys Res Commun. 2012 Aug 3;424(3):508-11. doi:, 10.1016/j.bbrc.2012.06.145. Epub 2012 Jul 3. PMID:22771800<ref>PMID:22771800</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3vu2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 1,4-alpha-glucan branching enzyme]]
 
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[[Category: Japanese rice]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chaen, K]]
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[[Category: Oryza sativa Japonica Group]]
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[[Category: Kakuta, Y]]
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[[Category: Chaen K]]
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[[Category: Kimura, M]]
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[[Category: Kakuta Y]]
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[[Category: Carbohydrate-binding module 48]]
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[[Category: Kimura M]]
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[[Category: Transferase]]
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Current revision

Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L

PDB ID 3vu2

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