5fip: Difference between revisions

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New page: '''Unreleased structure''' The entry 5fip is ON HOLD Authors: Zarafeta, D., Kissas, D., Sayer, C., Gudbergsdottir, S.R., Ladoukakis, E., Isupov, M.N., Chatziioannou, A., Peng, X., Littl...
 
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'''Unreleased structure'''


The entry 5fip is ON HOLD
==Discovery and characterization of a novel thermostable and highly halotolerant GH5 cellulase from an Icelandic hot spring isolate==
<StructureSection load='5fip' size='340' side='right'caption='[[5fip]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fip]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FIP 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]] 1.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=5fip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fip OCA], [https://pdbe.org/5fip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fip RCSB], [https://www.ebi.ac.uk/pdbsum/5fip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fip ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I3VS73_THESW I3VS73_THESW]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70 degrees C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics.


Authors: Zarafeta, D., Kissas, D., Sayer, C., Gudbergsdottir, S.R., Ladoukakis, E., Isupov, M.N., Chatziioannou, A., Peng, X., Littlechild, J.A., Skretas, G., Kolisis, F.N.
Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate.,Zarafeta D, Kissas D, Sayer C, Gudbergsdottir SR, Ladoukakis E, Isupov MN, Chatziioannou A, Peng X, Littlechild JA, Skretas G, Kolisis FN PLoS One. 2016 Jan 7;11(1):e0146454. doi: 10.1371/journal.pone.0146454., eCollection 2016. PMID:26741138<ref>PMID:26741138</ref>


Description: Discovery and characterization of a novel thermostable and highly halotolerant GH5 cellulase from an Icelandic hot spring isolate
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Ladoukakis, E]]
<div class="pdbe-citations 5fip" style="background-color:#fffaf0;"></div>
[[Category: Peng, X]]
== References ==
[[Category: Isupov, M.N]]
<references/>
[[Category: Skretas, G]]
__TOC__
[[Category: Gudbergsdottir, S.R]]
</StructureSection>
[[Category: Kolisis, F.N]]
[[Category: Large Structures]]
[[Category: Chatziioannou, A]]
[[Category: Unidentified]]
[[Category: Zarafeta, D]]
[[Category: Chatziioannou A]]
[[Category: Kissas, D]]
[[Category: Gudbergsdottir SR]]
[[Category: Littlechild, J.A]]
[[Category: Isupov MN]]
[[Category: Sayer, C]]
[[Category: Kissas D]]
[[Category: Kolisis FN]]
[[Category: Ladoukakis E]]
[[Category: Littlechild JA]]
[[Category: Peng X]]
[[Category: Sayer C]]
[[Category: Skretas G]]
[[Category: Zarafeta D]]

Latest revision as of 09:52, 19 July 2023

Discovery and characterization of a novel thermostable and highly halotolerant GH5 cellulase from an Icelandic hot spring isolateDiscovery and characterization of a novel thermostable and highly halotolerant GH5 cellulase from an Icelandic hot spring isolate

Structural highlights

5fip is a 4 chain structure with sequence from Unidentified. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.88Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

I3VS73_THESW

Publication Abstract from PubMed

With the ultimate goal of identifying robust cellulases for industrial biocatalytic conversions, we have isolated and characterized a new thermostable and very halotolerant GH5 cellulase. This new enzyme, termed CelDZ1, was identified by bioinformatic analysis from the genome of a polysaccharide-enrichment culture isolate, initiated from material collected from an Icelandic hot spring. Biochemical characterization of CelDZ1 revealed that it is a glycoside hydrolase with optimal activity at 70 degrees C and pH 5.0 that exhibits good thermostability, high halotolerance at near-saturating salt concentrations, and resistance towards metal ions and other denaturing agents. X-ray crystallography of the new enzyme showed that CelDZ1 is the first reported cellulase structure that lacks the defined sugar-binding 2 subsite and revealed structural features which provide potential explanations of its biochemical characteristics.

Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate.,Zarafeta D, Kissas D, Sayer C, Gudbergsdottir SR, Ladoukakis E, Isupov MN, Chatziioannou A, Peng X, Littlechild JA, Skretas G, Kolisis FN PLoS One. 2016 Jan 7;11(1):e0146454. doi: 10.1371/journal.pone.0146454., eCollection 2016. PMID:26741138[1]

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

References

  1. ↑ Zarafeta D, Kissas D, Sayer C, Gudbergsdottir SR, Ladoukakis E, Isupov MN, Chatziioannou A, Peng X, Littlechild JA, Skretas G, Kolisis FN. Discovery and Characterization of a Thermostable and Highly Halotolerant GH5 Cellulase from an Icelandic Hot Spring Isolate. PLoS One. 2016 Jan 7;11(1):e0146454. doi: 10.1371/journal.pone.0146454., eCollection 2016. PMID:26741138 doi:http://dx.doi.org/10.1371/journal.pone.0146454

5fip, resolution 1.88Å

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OCA
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