7a62
From Proteopedia
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==Structure of human indoleamine-2,3-dioxygenase 1 (hIDO1) with a complete JK loop== | ==Structure of human indoleamine-2,3-dioxygenase 1 (hIDO1) with a complete JK loop== | ||
| - | <StructureSection load='7a62' size='340' side='right'caption='[[7a62]]' scene=''> | + | <StructureSection load='7a62' size='340' side='right'caption='[[7a62]], [[Resolution|resolution]] 2.44Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6tue 6tue]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A62 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[7a62]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6tue 6tue]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A62 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IDO1, IDO, INDO ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Indoleamine_2,3-dioxygenase Indoleamine 2,3-dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.52 1.13.11.52] </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=7a62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a62 OCA], [https://pdbe.org/7a62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a62 RCSB], [https://www.ebi.ac.uk/pdbsum/7a62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a62 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/I23O1_HUMAN I23O1_HUMAN]] Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.<ref>PMID:17671174</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Indoleamine 2,3-dioxygenase 1 has sparked interest as an immunotherapeutic target in cancer research. Its structure includes a loop, named the JK-loop, that controls the orientation of the substrate or inhibitor within the active site. However, little has been reported about the crystal structure of this loop. In the present work, the conformation of the JK-loop is determined for the first time in the presence of the heme cofactor in the active site through X-ray diffraction experiments (2.44 A resolution). Molecular-dynamics trajectories were also obtained to provide dynamic information about the loop according to the presence of cofactor. This new structural and dynamic information highlights the importance of the JK-loop in confining the labile heme cofactor to the active site. | ||
| + | |||
| + | Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine 2,3-dioxygenase 1.,Mirgaux M, Leherte L, Wouters J Acta Crystallogr D Struct Biol. 2020 Dec 1;76(Pt 12):1211-1221. doi:, 10.1107/S2059798320013510. Epub 2020 Nov 19. PMID:33263327<ref>PMID:33263327</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7a62" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Indoleamine 2,3-dioxygenase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Mirgaux M]] | + | [[Category: Mirgaux, M]] |
| - | [[Category: Wouters J]] | + | [[Category: Wouters, J]] |
| + | [[Category: Dioxygenase]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Heme-binding]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Tryptophan catabolism]] | ||
Revision as of 17:54, 10 March 2021
Structure of human indoleamine-2,3-dioxygenase 1 (hIDO1) with a complete JK loop
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