3u9j

From Proteopedia

(Difference between revisions)

Revision as of 06:49, 5 August 2016

Crystal structure of oxidized human FBXL5 hemerythrin like domain

Structural highlights

3u9j is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	3u9m
Gene:	FBXL5, FBL4, FBL5, FLR1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3u9j"

@@ Line 1: / Line 1: @@
 ==Crystal structure of oxidized human FBXL5 hemerythrin like domain==
 <StructureSection load='3u9j' size='340' side='right' caption='[[3u9j]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3u9j]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3u9j]] is a 2 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=3U9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U9J FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u9m|3u9m]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBXL5, FBL4, FBL5, FLR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBXL5, FBL4, FBL5, FLR1 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u9j RCSB], [http://www.ebi.ac.uk/pdbsum/3u9j PDBsum]</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=3u9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u9j OCA], [http://pdbe.org/3u9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u9j RCSB], [http://www.ebi.ac.uk/pdbsum/3u9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u9j ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3u9j" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Li, P]]
 [[Category: Fbox]]

3u9j

From Proteopedia

Revision as of 06:49, 5 August 2016

Crystal structure of oxidized human FBXL5 hemerythrin like domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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