4ttc: Difference between revisions

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<StructureSection load='4ttc' size='340' side='right'caption='[[4ttc]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='4ttc' size='340' side='right'caption='[[4ttc]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ttc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TTC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TTC FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ttc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TTC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</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]] 2.65&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ttb|4ttb]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IYD, C6orf71, DEHAL1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ttc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ttc OCA], [https://pdbe.org/4ttc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ttc RCSB], [https://www.ebi.ac.uk/pdbsum/4ttc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ttc 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=4ttc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ttc OCA], [http://pdbe.org/4ttc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ttc RCSB], [http://www.ebi.ac.uk/pdbsum/4ttc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ttc ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/IYD1_HUMAN IYD1_HUMAN]] Familial thyroid dyshormonogenesis. The disease is caused by mutations affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/IYD1_HUMAN IYD1_HUMAN] Familial thyroid dyshormonogenesis. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/IYD1_HUMAN IYD1_HUMAN]] 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.<ref>PMID:15289438</ref> 
[https://www.uniprot.org/uniprot/IYD1_HUMAN IYD1_HUMAN] 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.<ref>PMID:15289438</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Reductive dehalogenation is not typical of aerobic organisms but plays a significant role in iodide homeostasis and thyroid activity. The flavoprotein iodotyrosine deiodinase (IYD) is responsible for iodide salvage by reductive deiodination of the iodotyrosine derivatives formed as byproducts of thyroid hormone biosynthesis. Heterologous expression of the human enzyme lacking its N-terminal membrane anchor has allowed for physical and biochemical studies to identify the role of substrate in controlling the active site geometry and flavin chemistry. Crystal structures of human IYD and its complex with 3-iodo-L-tyrosine illustrate the ability of the substrate to provide multiple interactions with the isoalloxazine system of FMN that are usually provided by protein side chains. Ligand binding acts to template the active site geometry and significantly stabilize the one electron reduced semiquinone form of FMN. The neutral form of this semiquinone is observed during reductive titration of IYD in the presence of the substrate analogue 3-fluoro-L-tyrosine. In the absence of an active site ligand, only the oxidized and two electron reduced forms of FMN are detected. The pH dependence of IYD binding and turnover also supports the importance of direct coordination between substrate and FMN for productive catalysis.
 
A Switch Between One- and Two-Electron Chemistry of the Human Flavoprotein Iodotyrosine Deiodinase is Controlled by Substrate.,Hu J, Chuenchor W, Rokita SE J Biol Chem. 2014 Nov 13. pii: jbc.M114.605964. PMID:25395621<ref>PMID:25395621</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ttc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Iodotyrosine deiodinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chuenchor, W]]
[[Category: Chuenchor W]]
[[Category: Hu, J]]
[[Category: Hu J]]
[[Category: Rokita, S]]
[[Category: Rokita S]]
[[Category: Dehalogenase]]
[[Category: Flavoprotein]]
[[Category: Iodide salvage]]
[[Category: Membrane]]
[[Category: Mit]]
[[Category: Mono-iodotyrosine]]
[[Category: Oxidoreductase]]
[[Category: Transmembrane]]

Latest revision as of 09:52, 3 April 2024

Crystal structure of homo sapiens IODOTYROSINE DEIODINASE bound to FMN and mono-iodotyrosine (MIT)Crystal structure of homo sapiens IODOTYROSINE DEIODINASE bound to FMN and mono-iodotyrosine (MIT)

Structural highlights

4ttc is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.65Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

IYD1_HUMAN Familial thyroid dyshormonogenesis. The disease is caused by mutations affecting the gene represented in this entry.

Function

IYD1_HUMAN 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.[1]

See Also

References

  1. ↑ Gnidehou S, Caillou B, Talbot M, Ohayon R, Kaniewski J, Noel-Hudson MS, Morand S, Agnangji D, Sezan A, Courtin F, Virion A, Dupuy C. Iodotyrosine dehalogenase 1 (DEHAL1) is a transmembrane protein involved in the recycling of iodide close to the thyroglobulin iodination site. FASEB J. 2004 Oct;18(13):1574-6. Epub 2004 Aug 2. PMID:15289438 doi:http://dx.doi.org/10.1096/fj.04-2023fje

4ttc, resolution 2.65Å

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