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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 ==
<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>
<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>
</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>
</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>
<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>
<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>
<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>
<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>
<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 ==
[[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.  
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vu2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 1,4-alpha-glucan branching enzyme]]
[[Category: Japanese rice]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chaen, K]]
[[Category: Oryza sativa Japonica Group]]
[[Category: Kakuta, Y]]
[[Category: Chaen K]]
[[Category: Kimura, M]]
[[Category: Kakuta Y]]
[[Category: Carbohydrate-binding module 48]]
[[Category: Kimura M]]
[[Category: Transferase]]

Latest revision as of 08:42, 20 March 2024

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

3vu2, resolution 2.23Å

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