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==Structure of intact chitinase with hevein domain from the plant Simarouba glauca, known for its traditional anti-inflammatory efficacy==
==Structure of intact chitinase with hevein domain from the plant Simarouba glauca, known for its traditional anti-inflammatory efficacy==
<StructureSection load='6lnr' size='340' side='right'caption='[[6lnr]]' scene=''>
<StructureSection load='6lnr' size='340' side='right'caption='[[6lnr]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LNR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LNR FirstGlance]. <br>
<table><tr><td colspan='2'>[[6lnr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Simarouba_glauca Simarouba glauca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LNR FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnr OCA], [http://pdbe.org/6lnr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lnr RCSB], [http://www.ebi.ac.uk/pdbsum/6lnr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnr ProSAT]</span></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]] 1.66&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6lnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lnr OCA], [https://pdbe.org/6lnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lnr RCSB], [https://www.ebi.ac.uk/pdbsum/6lnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lnr ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chitinase from the leaves of Simarouba glauca, a plant used in traditional anti-inflammatory therapy is purified and characterized. Peptide mass finger print analysis revealed the protein as an endo-chitinase which was further confirmed using chitin-agar assay. The enzyme exhibited significant anti-fungal efficacy against phyto-pathogens such as Macrophomina phaseolina, Fusarium oxysporum and Sclerotium rolfsii. Chitinolysis was also examined against insoluble chitin using SEM. Using X-ray diffraction data up to 1.66 A, the structure was determined by Molecular Replacement using crystal structure of GH19 Chitinase-like protein from Hevea brasiliensis. During structure refinement, an extra domain could be traced and identified as hevein domain. To our knowledge, this is the first report of any chitinase with intact hevein domain. The GH19 chitinase and hevein domains though connected by a lengthy loop, are restricted to be close by disulfide bridges. These bridges connecting each domain with the loop may be important for proper chitin feeding into the active site. By considering reports on hevein and chitinase domains as well as the traditional use of the plant, this report of an intact hevein-chitinase protein and their relative orientation may add further insights for the usefulness of this protein.
Structure of intact chitinase with hevein domain from the plant Simarouba glauca, known for its traditional anti-inflammatory efficacy.,Balu KE, Ramya KS, Radha A, Krishnasamy G Int J Biol Macromol. 2020 Oct 15;161:1381-1392. doi:, 10.1016/j.ijbiomac.2020.07.284. Epub 2020 Aug 1. PMID:32750481<ref>PMID:32750481</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lnr" style="background-color:#fffaf0;"></div>
==See Also==
*[[Chitinase 3D structures|Chitinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Simarouba glauca]]
[[Category: Ankur T]]
[[Category: Ankur T]]
[[Category: Gunasekaran K]]
[[Category: Gunasekaran K]]

Revision as of 17:38, 29 November 2023

Structure of intact chitinase with hevein domain from the plant Simarouba glauca, known for its traditional anti-inflammatory efficacyStructure of intact chitinase with hevein domain from the plant Simarouba glauca, known for its traditional anti-inflammatory efficacy

Structural highlights

6lnr is a 1 chain structure with sequence from Simarouba glauca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.66Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Chitinase from the leaves of Simarouba glauca, a plant used in traditional anti-inflammatory therapy is purified and characterized. Peptide mass finger print analysis revealed the protein as an endo-chitinase which was further confirmed using chitin-agar assay. The enzyme exhibited significant anti-fungal efficacy against phyto-pathogens such as Macrophomina phaseolina, Fusarium oxysporum and Sclerotium rolfsii. Chitinolysis was also examined against insoluble chitin using SEM. Using X-ray diffraction data up to 1.66 A, the structure was determined by Molecular Replacement using crystal structure of GH19 Chitinase-like protein from Hevea brasiliensis. During structure refinement, an extra domain could be traced and identified as hevein domain. To our knowledge, this is the first report of any chitinase with intact hevein domain. The GH19 chitinase and hevein domains though connected by a lengthy loop, are restricted to be close by disulfide bridges. These bridges connecting each domain with the loop may be important for proper chitin feeding into the active site. By considering reports on hevein and chitinase domains as well as the traditional use of the plant, this report of an intact hevein-chitinase protein and their relative orientation may add further insights for the usefulness of this protein.

Structure of intact chitinase with hevein domain from the plant Simarouba glauca, known for its traditional anti-inflammatory efficacy.,Balu KE, Ramya KS, Radha A, Krishnasamy G Int J Biol Macromol. 2020 Oct 15;161:1381-1392. doi:, 10.1016/j.ijbiomac.2020.07.284. Epub 2020 Aug 1. PMID:32750481[1]

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

See Also

References

  1. Balu KE, Ramya KS, Radha A, Krishnasamy G. Structure of intact chitinase with hevein domain from the plant Simarouba glauca, known for its traditional anti-inflammatory efficacy. Int J Biol Macromol. 2020 Oct 15;161:1381-1392. PMID:32750481 doi:10.1016/j.ijbiomac.2020.07.284

6lnr, resolution 1.66Å

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OCA