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| | ==Crystal structure of Mus musculus iodotyrosine deiodinase (IYD) C217A, C239A bound to FMN== | | ==Crystal structure of Mus musculus iodotyrosine deiodinase (IYD) C217A, C239A bound to FMN== |
| - | <StructureSection load='3to0' size='340' side='right' caption='[[3to0]], [[Resolution|resolution]] 2.66Å' scene=''> | + | <StructureSection load='3to0' size='340' side='right'caption='[[3to0]], [[Resolution|resolution]] 2.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3to0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TO0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3to0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TO0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.655Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gb5|3gb5]], [[3gfd|3gfd]], [[3gh8|3gh8]], [[3tnz|3tnz]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IYD-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3to0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to0 OCA], [https://pdbe.org/3to0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3to0 RCSB], [https://www.ebi.ac.uk/pdbsum/3to0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3to0 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Iodotyrosine_deiodinase Iodotyrosine deiodinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.22.1.1 1.22.1.1] </span></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=3to0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to0 OCA], [http://pdbe.org/3to0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3to0 RCSB], [http://www.ebi.ac.uk/pdbsum/3to0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3to0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IYD1_MOUSE IYD1_MOUSE]] Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine (By similarity). | + | [https://www.uniprot.org/uniprot/IYD1_MOUSE IYD1_MOUSE] Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine (By similarity). |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Reductive deiodination is critical for thyroid function and represents an unusual exception to the more common oxidative and hydrolytic mechanisms of dehalogenation in mammals. Studies on the reductive processes have been limited by a lack of convenient methods for heterologous expression of the appropriate proteins in large scale. The enzyme responsible for iodide salvage in the thyroid, iodotyrosine deodinase, is now readily generated after engineering its gene from Mus musculus. High expression of a truncated derivative lacking the membrane domain at its N-terminal was observed in Sf9 cells whereas expression in Pichia pastoris remained low despite codon optimization. Ultimately, the desired expression in Escherichia coli was achieved after replacing the two conserved Cys residues of the deiodinase with Ala and fusing the resulting protein to thioredoxin. This final construct provided abundant enzyme for crystallography and mutagenesis. Utility of the E. coli system was demonstrated by examining a set of active site residues critical for binding to the zwitterionic portion of substrate.
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| - | Expression of a soluble form of iodotyrosine deiodinase for active site characterization by engineering the native membrane protein from mus musculus.,Buss JM, McTamney PM, Rokita TE Protein Sci. 2012 Jan 11. doi: 10.1002/pro.2020. PMID:22238141<ref>PMID:22238141</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3to0" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Dehalogenase|Dehalogenase]] | + | *[[Dehalogenase 3D structures|Dehalogenase 3D structures]] |
| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Iodotyrosine deiodinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Buss, J M]] | + | [[Category: Buss JM]] |
| - | [[Category: McTamney, P M]] | + | [[Category: McTamney PM]] |
| - | [[Category: Rokita, S E]] | + | [[Category: Rokita SE]] |
| - | [[Category: Dehalogenase]]
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| - | [[Category: Flavoprotein]]
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| - | [[Category: Iodide salvage]]
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| - | [[Category: Membrane]]
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| - | [[Category: Mono-iodotyrosine]]
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| - | [[Category: Nadp]]
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| - | [[Category: Oxidoreductase]]
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| - | [[Category: Transmembrane]]
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