3sn2: Difference between revisions

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 ==Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNA==
-<StructureSection load='3sn2' size='340' side='right' caption='[[3sn2]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
+<StructureSection load='3sn2' size='340' side='right'caption='[[3sn2]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sn2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SN2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sn2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SN2 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ipy|2ipy]], [[3snp|3snp]]</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]] 2.99&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACO1, FRP, IREB1, IREBP, IRP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</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=3sn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sn2 OCA], [https://pdbe.org/3sn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sn2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sn2 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/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3] </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=3sn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sn2 OCA], [http://pdbe.org/3sn2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sn2 RCSB], [http://www.ebi.ac.uk/pdbsum/3sn2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sn2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACOC_RABIT ACOC_RABIT]] Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding (By similarity).  Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity).
+[https://www.uniprot.org/uniprot/ACOHC_RABIT ACOHC_RABIT] Bifunctional iron sensor that switches between 2 activities depending on iron availability (By similarity). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization (PubMed:17185597). Binds to iron-responsive elements (IRES) in the untranslated region of target mRNAs preventing for instance the translation of ferritin and aminolevulinic acid synthase and stabilizing the transferrin receptor mRNA (PubMed:17185597).[UniProtKB:P21399]<ref>PMID:17185597</ref>   Conversely, when cellular iron levels are high, binds a 4Fe-4S cluster which precludes RNA binding activity and promotes the aconitase activity, the isomerization of citrate to isocitrate via cis-aconitate.[UniProtKB:P21399]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Iron responsive elements (IREs) are short stem-loop structures found in several mRNAs encoding proteins involved in cellular iron metabolism. Iron regulatory proteins (IRPs) control iron homeostasis through differential binding to the IREs, accommodating any sequence or structural variations that the IREs may present. Here we report the structure of IRP1 in complex with transferrin receptor 1 B (TfR B) IRE, and compare it to the complex with ferritin H (Ftn H) IRE. The two IREs are bound to IRP1 through nearly identical protein-RNA contacts, although their stem conformations are significantly different. These results support the view that binding of different IREs with IRP1 depends both on protein and RNA conformational plasticity, adapting to RNA variation while retaining conserved protein-RNA contacts.
-Accommodating variety in iron-responsive elements: Crystal structure of transferrin receptor 1 B IRE bound to iron regulatory protein 1.,Walden WE, Selezneva A, Volz K FEBS Lett. 2012 Jan 2;586(1):32-5. Epub 2011 Nov 24. PMID:22119729<ref>PMID:22119729</ref>
+==See Also==
+*[[Aconitase 3D structures|Aconitase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3sn2" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aconitate hydratase]]
+[[Category: Large Structures]]
-[[Category: European rabbit]]
+[[Category: Oryctolagus cuniculus]]
-[[Category: Selezneva, A I]]
+[[Category: Selezneva AI]]
-[[Category: Volz, K]]
+[[Category: Volz K]]
-[[Category: Walden, W E]]
+[[Category: Walden WE]]
-[[Category: Iron sulfur cluster binding]]
-[[Category: Lyase-rna complex]]
-[[Category: Phosphorylation]]
-[[Category: Rna binding]]