7rei

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Current revision (07:19, 3 April 2024) (edit) (undo)
 
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<StructureSection load='7rei' size='340' side='right'caption='[[7rei]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='7rei' size='340' side='right'caption='[[7rei]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7rei]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7REI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7REI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7rei]] is a 1 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=7REI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7REI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 1.78&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cysteamine_dioxygenase Cysteamine dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.19 1.13.11.19] </span></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=7rei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rei OCA], [https://pdbe.org/7rei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rei RCSB], [https://www.ebi.ac.uk/pdbsum/7rei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rei ProSAT]</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=7rei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rei OCA], [https://pdbe.org/7rei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rei RCSB], [https://www.ebi.ac.uk/pdbsum/7rei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rei ProSAT]</span></td></tr>
</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/AEDO_HUMAN AEDO_HUMAN]
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Cysteamine dioxygenase (ADO) plays a vital role in regulating thiol metabolism and preserving oxygen homeostasis in humans by oxidizing the sulfur of cysteamine and N-terminal cysteine-containing proteins to their corresponding sulfinic acids using O2 as a cosubstrate. However, as the only thiol dioxygenase that processes both small-molecule and protein substrates, how ADO handles diverse substrates of disparate sizes to achieve various reactions is not understood. The knowledge gap is mainly due to the three-dimensional structure not being solved, as ADO cannot be directly compared with other known thiol dioxygenases. Herein, we report the first crystal structure of human ADO at a resolution of 1.78 A with a nickel-bound metal center. Crystallization was achieved through both metal substitution and C18S/C239S double mutations. The metal center resides in a tunnel close to an entry site flanked by loops. While ADO appears to use extensive flexibility to handle substrates of different sizes, it also employs proline and proline pairs to maintain the core protein structure and to retain the residues critical for catalysis in place. This feature distinguishes ADO from thiol dioxygenases oxidizing that only oxidize small-molecule substrates, possibly explaining its divergent substrate specificity. Our findings also elucidate the structural basis for ADO functioning as an oxygen sensor by modifying N-degron substrates to transduce responses to hypoxia. Thus, this work fills a gap in structure-function relationships of the thiol dioxygenase family and provides a platform for further mechanistic investigation and therapeutic intervention targeting impaired oxygen sensing.
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Crystal Structure of Human Cysteamine Dioxygenase Provides a Structural Rationale for its Function as an Oxygen Sensor.,Wang YA, Shin I, Li J, Liu A J Biol Chem. 2021 Sep 8:101176. doi: 10.1016/j.jbc.2021.101176. PMID:34508780<ref>PMID:34508780</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 7rei" 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: Cysteamine dioxygenase]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, J]]
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[[Category: Li J]]
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[[Category: Liu, A]]
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[[Category: Liu A]]
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[[Category: Shin, I]]
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[[Category: Shin I]]
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[[Category: Wang, Y]]
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[[Category: Wang Y]]
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[[Category: Non-heme iron-dependent dioxygenase]]
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[[Category: Oxidoreductase]]
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Current revision

The crystal structure of nickel bound human ADO C18S C239S variant

PDB ID 7rei

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OCA

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