6rv5: Difference between revisions

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'''Unreleased structure'''


The entry 6rv5 is ON HOLD  until Paper Publication
==X-ray structure of the levansucrase from Erwinia tasmaniensis in complex with levanbiose==
<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 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='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='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'>[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 ==
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.


Authors: Polsinelli, I., Caliandro, R., Demitri, N., Benini, S.
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>


Description: X-ray structure of the levansucrase from Erwinia tasmaniensis in complex with levanbiose
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Caliandro, R]]
<div class="pdbe-citations 6rv5" style="background-color:#fffaf0;"></div>
[[Category: Polsinelli, I]]
== References ==
[[Category: Demitri, N]]
<references/>
[[Category: Benini, S]]
__TOC__
</StructureSection>
[[Category: Erwinia tasmaniensis Et1/99]]
[[Category: Large Structures]]
[[Category: Benini S]]
[[Category: Caliandro R]]
[[Category: Demitri N]]
[[Category: Polsinelli I]]

Latest revision as of 14:51, 1 February 2024

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

6rv5 is a 1 chain structure with sequence from Erwinia tasmaniensis Et1/99. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.58Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B2VCC3_ERWT9

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Polsinelli I, Caliandro R, Demitri N, Benini S. The Structure of Sucrose-Soaked Levansucrase Crystals from Erwinia tasmaniensis reveals a Binding Pocket for Levanbiose. Int J Mol Sci. 2019 Dec 20;21(1). pii: ijms21010083. doi: 10.3390/ijms21010083. PMID:31877648 doi:http://dx.doi.org/10.3390/ijms21010083

6rv5, resolution 1.58Å

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