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| <StructureSection load='3om6' size='340' side='right'caption='[[3om6]], [[Resolution|resolution]] 1.96Å' scene=''> | | <StructureSection load='3om6' size='340' side='right'caption='[[3om6]], [[Resolution|resolution]] 1.96Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3om6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OM6 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3om6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OM6 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.96Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3om2|3om2]], [[3om4|3om4]], [[3om5|3om5]], [[3om7|3om7]]</div></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sacB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr> | |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Levansucrase Levansucrase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.10 2.4.1.10] </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=3om6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3om6 OCA], [https://pdbe.org/3om6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3om6 RCSB], [https://www.ebi.ac.uk/pdbsum/3om6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3om6 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=3om6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3om6 OCA], [https://pdbe.org/3om6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3om6 RCSB], [https://www.ebi.ac.uk/pdbsum/3om6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3om6 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/D5DC07_PRIM3 D5DC07_PRIM3] |
| Despite the widespread biological function of carbohydrates, the polysaccharide synthesis mechanisms of glycosyltransferases remain largely unexplored. Bacterial levansucrases (glycoside hydrolase family 68) synthesize high molecular weight, beta-(2,6)-linked levan from sucrose by transfer of fructosyl units. The kinetic and biochemical characterization of Bacillus megaterium levansucrase SacB variants Y247A, Y247W, N252A, D257A, and K373A reveal novel surface motifs remote from the sucrose binding site with distinct influence on the polysaccharide product spectrum. The wild type activity (k(cat)) and substrate affinity (K(m)) are maintained. The structures of the SacB variants reveal clearly distinguishable subsites for polysaccharide synthesis as well as an intact active site architecture. These results lead to a new understanding of polysaccharide synthesis mechanisms. The identified surface motifs are discussed in the context of related glycosyltransferases.
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| Polysaccharide Synthesis of the Levansucrase SacB from Bacillus megaterium Is Controlled by Distinct Surface Motifs.,Strube CP, Homann A, Gamer M, Jahn D, Seibel J, Heinz DW J Biol Chem. 2011 May 20;286(20):17593-600. Epub 2011 Mar 25. PMID:21454585<ref>PMID:21454585</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3om6" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 14581]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Levansucrase]] | | [[Category: Priestia megaterium]] |
| [[Category: Gamer, M]] | | [[Category: Gamer M]] |
| [[Category: Heinz, D W]] | | [[Category: Heinz DW]] |
| [[Category: Homann, A]] | | [[Category: Homann A]] |
| [[Category: Jahn, D]] | | [[Category: Jahn D]] |
| [[Category: Seibel, J]] | | [[Category: Seibel J]] |
| [[Category: Strube, C P]] | | [[Category: Strube CP]] |
| [[Category: Five fold beta-propeller]]
| |
| [[Category: Transferase]]
| |