4ilv

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==Structure of the dioxygenase domain of SACTE_2871, a novel dioxygenase carbohydrate-binding protein fusion from the cellulolytic bacterium Streptomyces sp. SirexAA-E==
==Structure of the dioxygenase domain of SACTE_2871, a novel dioxygenase carbohydrate-binding protein fusion from the cellulolytic bacterium Streptomyces sp. SirexAA-E==
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<StructureSection load='4ilv' size='340' side='right' caption='[[4ilv]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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<StructureSection load='4ilv' size='340' side='right'caption='[[4ilv]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ilv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strek Strek]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ILV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ILV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ilv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._SirexAA-E Streptomyces sp. SirexAA-E]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ILV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ILV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ilt|4ilt]], [[4ily|4ily]], [[4im1|4im1]], [[4im4|4im4]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SACTE_2871 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=862751 STREK])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ilv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ilv OCA], [https://pdbe.org/4ilv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ilv RCSB], [https://www.ebi.ac.uk/pdbsum/4ilv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ilv ProSAT]</span></td></tr>
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<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=4ilv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ilv OCA], [http://pdbe.org/4ilv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ilv RCSB], [http://www.ebi.ac.uk/pdbsum/4ilv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ilv ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G2NEL6_STREK G2NEL6_STREK]
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Streptomyces sp. SirexAA-E is a highly cellulolytic bacterium isolated from an insect/microbe symbiotic community. When grown on lignin-containing biomass, it secretes SACTE_2871, an aromatic ring dioxygenase domain fused to a family 5/12 carbohydrate-binding module (CBM 5/12). Here we present structural and catalytic studies of this novel fusion enzyme, thus providing insight into its function. The dioxygenase domain has the core beta sandwich fold typical of this enzyme family but lacks a dimerization domain observed in other intradiol dioxygenases. Consequently, the X-ray structure shows that the enzyme is monomeric and the Fe(III)-containing active site is exposed to solvent in a shallow depression on a planar surface. Purified SACTE_2871 catalyzes the O2-dependent intradiol cleavage of catecholic compounds from lignin biosynthetic pathways, but not their methoxylated derivatives. Binding studies show that SACTE_2871 binds synthetic lignin polymers and chitin through the interactions of the CBM 5/12 domain, representing a new binding specificity for this fold family. Based on its unique structural features and functional properties, we propose that SACTE_2871 contributes to the invasive nature of the insect/microbial community by destroying precursors needed by the plant for de novo lignin biosynthesis as part of its natural wounding response.
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Fusion of dioxygenase and lignin-binding domains in a novel secreted enzyme from cellulolytic Streptomyces sp. SirexAA-E.,Bianchetti CM, Harmann CH, Takasuka TE, Hura GL, Dyer K, Fox BG J Biol Chem. 2013 May 7. PMID:23653358<ref>PMID:23653358</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4ilv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Strek]]
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[[Category: Large Structures]]
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[[Category: Bergeman, L F]]
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[[Category: Streptomyces sp. SirexAA-E]]
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[[Category: Bianchetti, C M]]
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[[Category: Bergeman LF]]
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[[Category: Fox, B G]]
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[[Category: Bianchetti CM]]
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[[Category: Harmann, C H]]
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[[Category: Fox BG]]
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[[Category: Takasuka, T E]]
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[[Category: Harmann CH]]
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[[Category: Carbohydrate binding domain]]
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[[Category: Takasuka TE]]
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[[Category: Intradiol dioxygenase]]
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[[Category: Iron center]]
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[[Category: Oxidoreductase]]
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Current revision

Structure of the dioxygenase domain of SACTE_2871, a novel dioxygenase carbohydrate-binding protein fusion from the cellulolytic bacterium Streptomyces sp. SirexAA-E

PDB ID 4ilv

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