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| | <StructureSection load='3u9j' size='340' side='right'caption='[[3u9j]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='3u9j' size='340' side='right'caption='[[3u9j]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3u9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3u9j]] is a 2 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=3U9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U9J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.603Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3u9m|3u9m]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBXL5, FBL4, FBL5, FLR1 ([https://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=3u9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9j OCA], [https://pdbe.org/3u9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9j RCSB], [https://www.ebi.ac.uk/pdbsum/3u9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9j 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=3u9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9j OCA], [https://pdbe.org/3u9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u9j RCSB], [https://www.ebi.ac.uk/pdbsum/3u9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FBXL5_HUMAN FBXL5_HUMAN]] Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.<ref>PMID:17532294</ref> <ref>PMID:19762596</ref> <ref>PMID:19762597</ref>
| + | [https://www.uniprot.org/uniprot/FBXL5_HUMAN FBXL5_HUMAN] Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.<ref>PMID:17532294</ref> <ref>PMID:19762596</ref> <ref>PMID:19762597</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, P]] | + | [[Category: Li P]] |
| - | [[Category: Fbox]]
| + | |
| - | [[Category: Iron sensor]]
| + | |
| - | [[Category: Lrr]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Ubiquitin ligase e3]]
| + | |
| Structural highlights
Function
FBXL5_HUMAN Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2. Upon high iron and oxygen level, it specifically recognizes and binds IREB2/IRP2, promoting its ubiquitination and degradation by the proteasome. Promotes ubiquitination and subsequent degradation of DCTN1/p150-glued.[1] [2] [3]
Publication Abstract from PubMed
Iron sensing: The F-box and leucine-rich repeat containing protein FBXL5 is an iron sensor that regulates the ubiquitination of iron regulatory protein IRP2. Crystal structures of the iron-sensing hemetrythrin (Hr)-like domain of human FBXL5 (FBXL5 Hr) were determined in oxidized and reduced states. These structures revealed the mechanisms of iron sensing by FBXL5.
The Structural Basis of Iron Sensing by the Human F-box Protein FBXL5.,Shu C, Sung MW, Stewart MD, Igumenova TI, Tan X, Li P Chembiochem. 2012 Apr 16;13(6):788-91. doi: 10.1002/cbic.201200043. PMID:22492618[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang N, Liu J, Ding X, Aikhionbare F, Jin C, Yao X. FBXL5 interacts with p150Glued and regulates its ubiquitination. Biochem Biophys Res Commun. 2007 Jul 20;359(1):34-9. Epub 2007 May 21. PMID:17532294 doi:http://dx.doi.org/10.1016/j.bbrc.2007.05.068
- ↑ Vashisht AA, Zumbrennen KB, Huang X, Powers DN, Durazo A, Sun D, Bhaskaran N, Persson A, Uhlen M, Sangfelt O, Spruck C, Leibold EA, Wohlschlegel JA. Control of iron homeostasis by an iron-regulated ubiquitin ligase. Science. 2009 Oct 30;326(5953):718-21. Epub 2009 Sep 17. PMID:19762596 doi:http://dx.doi.org/1176333
- ↑ Salahudeen AA, Thompson JW, Ruiz JC, Ma HW, Kinch LN, Li Q, Grishin NV, Bruick RK. An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis. Science. 2009 Oct 30;326(5953):722-6. Epub 2009 Sep 17. PMID:19762597 doi:10.1126/science.1176326
- ↑ Shu C, Sung MW, Stewart MD, Igumenova TI, Tan X, Li P. The Structural Basis of Iron Sensing by the Human F-box Protein FBXL5. Chembiochem. 2012 Apr 16;13(6):788-91. doi: 10.1002/cbic.201200043. PMID:22492618 doi:10.1002/cbic.201200043
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