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| | ==Structure of barley starch synthase I in complex with maltooligosaccharide== | | ==Structure of barley starch synthase I in complex with maltooligosaccharide== |
| - | <StructureSection load='4hln' size='340' side='right' caption='[[4hln]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4hln' size='340' side='right'caption='[[4hln]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hln]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Barley Barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HLN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hln]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HLN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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">SSI, glgA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4513 Barley])</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=4hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hln OCA], [https://pdbe.org/4hln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hln RCSB], [https://www.ebi.ac.uk/pdbsum/4hln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hln ProSAT]</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 Starch synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.21 2.4.1.21] </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=4hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hln OCA], [http://pdbe.org/4hln PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hln RCSB], [http://www.ebi.ac.uk/pdbsum/4hln PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hln ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9M5A3_HORVU Q9M5A3_HORVU] |
| | <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: Barley]] | + | [[Category: Hordeum vulgare]] |
| - | [[Category: Starch synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Cuesta-Seijo, J A]] | + | [[Category: Cuesta-Seijo JA]] |
| - | [[Category: Marri, L]] | + | [[Category: Marri L]] |
| - | [[Category: Nielsen, M M]] | + | [[Category: Nielsen MM]] |
| - | [[Category: Palcic, M M]] | + | [[Category: Palcic MM]] |
| - | [[Category: Tanaka, H]] | + | [[Category: Tanaka H]] |
| - | [[Category: Adpglucose]]
| + | |
| - | [[Category: Amylopectin]]
| + | |
| - | [[Category: Disulfide]]
| + | |
| - | [[Category: Double rossmann fold]]
| + | |
| - | [[Category: Glycogen]]
| + | |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Maltooligosaccharide]]
| + | |
| - | [[Category: Plastidial]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9M5A3_HORVU
Publication Abstract from PubMed
Starch, a polymer of glucose, is the major source of calories in the human diet. It has numerous industrial uses, including as a raw material for the production of first-generation bioethanol. Several classes of enzymes take part in starch biosynthesis, of which starch synthases (SSs) carry out chain elongation of both amylose and amylopectin. Plants have five classes of SS, each with different roles. The products of the reaction of SS are well known, but details of the reaction mechanism remain obscure and even less is known of how different SSs select different substrates for elongation, how they compete with each other and how their activities are regulated. Here, the first crystal structure of a soluble starch synthase is presented: that of starch synthase I (SSI) from barley refined to 2.7 A resolution. The structure captures an open conformation of the enzyme with a surface-bound maltooligosaccharide and a disulfide bridge that precludes formation of the active site. The maltooligosaccharide-binding site is involved in substrate recognition, while the disulfide bridge is reflective of redox regulation of SSI. Activity measurements on several SSI mutants supporting these roles are also presented.
Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity.,Cuesta-Seijo JA, Nielsen MM, Marri L, Tanaka H, Beeren SR, Palcic MM Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1013-25. doi:, 10.1107/S090744491300440X. Epub 2013 May 14. PMID:23695246[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cuesta-Seijo JA, Nielsen MM, Marri L, Tanaka H, Beeren SR, Palcic MM. Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity. Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1013-25. doi:, 10.1107/S090744491300440X. Epub 2013 May 14. PMID:23695246 doi:10.1107/S090744491300440X
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