6rv5: Difference between revisions
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<StructureSection load='6rv5' size='340' side='right'caption='[[6rv5]], [[Resolution|resolution]] 1.58Å' scene=''> | <StructureSection load='6rv5' size='340' side='right'caption='[[6rv5]], [[Resolution|resolution]] 1.58Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6rv5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RV5 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[6rv5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Erwt9 Erwt9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RV5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RV5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lsc, ETA_34670 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=465817 ERWT9])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Levansucrase Levansucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.10 2.4.1.10] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Levansucrase Levansucrase], with EC number [http://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'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rv5 OCA], [http://pdbe.org/6rv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rv5 RCSB], [http://www.ebi.ac.uk/pdbsum/6rv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rv5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Given its potential role in the synthesis of novel prebiotics and applications in the pharmaceutical industry, a strong interest has developed in the enzyme levansucrase (LSC, EC 2.4.1.10). LSC catalyzes both the hydrolysis of sucrose (or sucroselike substrates) and the transfructosylation of a wide range of acceptors. LSC from the Gram-negative bacterium Erwinia tasmaniensis (EtLSC) is an interesting biocatalyst due to its high-yield production of fructooligosaccharides (FOSs). In order to learn more about the process of chain elongation, we obtained the crystal structure of EtLSC in complex with levanbiose (LBS). LBS is an FOS intermediate formed during the synthesis of longer-chain FOSs and levan. Analysis of the LBS binding pocket revealed that its structure was conserved in several related species. The binding pocket discovered in this crystal structure is an ideal target for future mutagenesis studies in order to understand its biological relevance and to engineer LSCs into tailored products. | |||
The Structure of Sucrose-Soaked Levansucrase Crystals from Erwinia tasmaniensis reveals a Binding Pocket for Levanbiose.,Polsinelli I, Caliandro R, Demitri N, Benini S Int J Mol Sci. 2019 Dec 20;21(1). pii: ijms21010083. doi: 10.3390/ijms21010083. PMID:31877648<ref>PMID:31877648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Erwt9]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Levansucrase]] | [[Category: Levansucrase]] | ||
Revision as of 10:22, 8 April 2020
X-ray structure of the levansucrase from Erwinia tasmaniensis in complex with levanbioseX-ray structure of the levansucrase from Erwinia tasmaniensis in complex with levanbiose
Structural highlights
Publication Abstract from PubMedGiven its potential role in the synthesis of novel prebiotics and applications in the pharmaceutical industry, a strong interest has developed in the enzyme levansucrase (LSC, EC 2.4.1.10). LSC catalyzes both the hydrolysis of sucrose (or sucroselike substrates) and the transfructosylation of a wide range of acceptors. LSC from the Gram-negative bacterium Erwinia tasmaniensis (EtLSC) is an interesting biocatalyst due to its high-yield production of fructooligosaccharides (FOSs). In order to learn more about the process of chain elongation, we obtained the crystal structure of EtLSC in complex with levanbiose (LBS). LBS is an FOS intermediate formed during the synthesis of longer-chain FOSs and levan. Analysis of the LBS binding pocket revealed that its structure was conserved in several related species. The binding pocket discovered in this crystal structure is an ideal target for future mutagenesis studies in order to understand its biological relevance and to engineer LSCs into tailored products. The Structure of Sucrose-Soaked Levansucrase Crystals from Erwinia tasmaniensis reveals a Binding Pocket for Levanbiose.,Polsinelli I, Caliandro R, Demitri N, Benini S Int J Mol Sci. 2019 Dec 20;21(1). pii: ijms21010083. doi: 10.3390/ijms21010083. PMID:31877648[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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