6rv5: Difference between revisions

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 <StructureSection load='6rv5' size='340' side='right'caption='[[6rv5]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
 == 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RV5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6rv5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Erwinia_tasmaniensis_Et1/99 Erwinia tasmaniensis Et1/99]. 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 [https://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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</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='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=PRD_900051:levanbiose'>PRD_900051</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rv5 OCA], [https://pdbe.org/6rv5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rv5 RCSB], [https://www.ebi.ac.uk/pdbsum/6rv5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rv5 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/B2VCC3_ERWT9 B2VCC3_ERWT9]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
-Erwinia tasmaniensis is an epiphytic bacterium related to the plant pathogen Erwinia amylovora, the etiological agent of fire blight. In this study the levansucrase from E. tasmaniensis (EtLsc) has been compared with the homologous enzyme from E. amylovora (EaLsc). We characterized the enzymatic activity and compared the products profile of both enzymes by High Performance Anion Exchange Chromatography coupled with Pulsed Amperometric Detector (HPAEC-PAD). Moreover we determined the crystal structure of EtLsc to understand the structural peculiarity causing the different product profiles of the two homologues. EtLsc exhibits increased efficiency in the production of FOS, resulting in a better catalyst for biotechnological synthesis than EaLsc. Based on our results, we propose that the role of this enzyme in the life cycle of the two bacteria is most likely related to survival, rather than linked to pathogenicity in E. amylovora.
+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.
-Comparison of the Levansucrase from the epiphyte Erwinia tasmaniensis vs its homologue from the phytopathogen Erwinia amylovora.,Polsinelli I, Caliandro R, Salomone-Stagni M, Demitri N, Rejzek M, Field RA, Benini S Int J Biol Macromol. 2019 Apr 15;127:496-501. doi:, 10.1016/j.ijbiomac.2019.01.074. Epub 2019 Jan 17. PMID:30660564<ref>PMID:30660564</ref>
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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 __TOC__
 </StructureSection>
+[[Category: Erwinia tasmaniensis Et1/99]]
 [[Category: Large Structures]]
-[[Category: Levansucrase]]
+[[Category: Benini S]]
-[[Category: Benini, S]]
+[[Category: Caliandro R]]
-[[Category: Caliandro, R]]
+[[Category: Demitri N]]
-[[Category: Demitri, N]]
+[[Category: Polsinelli I]]
-[[Category: Polsinelli, I]]
-[[Category: Fructans production]]
-[[Category: Fructosyltransferase]]
-[[Category: Levanbiose]]
-[[Category: Transferase]]