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==Manganese Superoxide Dismutase from Sphingobacterium sp. T2==
==Manganese Superoxide Dismutase from Sphingobacterium sp. T2==
<StructureSection load='5a9g' size='340' side='right' caption='[[5a9g]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='5a9g' size='340' side='right'caption='[[5a9g]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5a9g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A9G FirstGlance]. <br>
<table><tr><td colspan='2'>[[5a9g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingobacterium_spiritivorum Sphingobacterium spiritivorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A9G FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.35&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a9g RCSB], [http://www.ebi.ac.uk/pdbsum/5a9g PDBsum]</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=5a9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a9g OCA], [https://pdbe.org/5a9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a9g RCSB], [https://www.ebi.ac.uk/pdbsum/5a9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a9g ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3KL50_SPHSI A0A0M3KL50_SPHSI] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 5a9g" style="background-color:#fffaf0;"></div>
==See Also==
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Superoxide dismutase]]
[[Category: Large Structures]]
[[Category: Bugg, T D.H]]
[[Category: Sphingobacterium spiritivorum]]
[[Category: Fulop, V]]
[[Category: Bugg TDH]]
[[Category: Liu, Y]]
[[Category: Fulop V]]
[[Category: Rashid, G M.M]]
[[Category: Liu Y]]
[[Category: Rea, D]]
[[Category: Rashid GMM]]
[[Category: Taylor, C R]]
[[Category: Rea D]]
[[Category: Zhang, X]]
[[Category: Taylor CR]]
[[Category: Lignin oxidation]]
[[Category: Zhang X]]
[[Category: Lignin valorisation]]
[[Category: Manganese superoxide dismutase]]
[[Category: Oxidoreductase]]
[[Category: Sphingobacterium]]

Latest revision as of 14:06, 10 January 2024

Manganese Superoxide Dismutase from Sphingobacterium sp. T2Manganese Superoxide Dismutase from Sphingobacterium sp. T2

Structural highlights

5a9g is a 2 chain structure with sequence from Sphingobacterium spiritivorum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.35Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0M3KL50_SPHSI Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]

Publication Abstract from PubMed

The valorization of aromatic heteropolymer lignin is an important unsolved problem in the development of a biomass-based biorefinery, for which novel high-activity biocatalysts are needed. Sequencing of the genomic DNA of lignin-degrading bacterial strain Sphingobacterium sp. T2 revealed no matches to known lignin-degrading genes. Proteomic matches for two manganese superoxide dismutase proteins were found in partially purified extracellular fractions. Recombinant MnSOD1 and MnSOD2 were both found to show high activity for oxidation of Organosolv and Kraft lignin, and lignin model compounds, generating multiple oxidation products. Structure determination revealed that the products result from aryl-Calpha and Calpha-Cbeta bond oxidative cleavage and O-demethylation. The crystal structure of MnSOD1 was determined to 1.35 A resolution, revealing a typical MnSOD homodimer harboring a five-coordinate trigonal bipyramidal Mn(II) center ligated by three His, one Asp, and a water/hydroxide in each active site. We propose that the lignin oxidation reactivity of these enzymes is due to the production of a hydroxyl radical, a highly reactive oxidant. This is the first demonstration that MnSOD is a microbial lignin-oxidizing enzyme.

Identification of Manganese Superoxide Dismutase from Sphingobacterium sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation.,Rashid GM, Taylor CR, Liu Y, Zhang X, Rea D, Fulop V, Bugg TD ACS Chem Biol. 2015 Aug 3. PMID:26198187[1]

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

See Also

References

  1. Rashid GM, Taylor CR, Liu Y, Zhang X, Rea D, Fulop V, Bugg TD. Identification of Manganese Superoxide Dismutase from Sphingobacterium sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation. ACS Chem Biol. 2015 Aug 3. PMID:26198187 doi:http://dx.doi.org/10.1021/acschembio.5b00298

5a9g, resolution 1.35Å

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