3sn2

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==Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNA==
==Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNA==
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<StructureSection load='3sn2' size='340' side='right' caption='[[3sn2]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
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<StructureSection load='3sn2' size='340' side='right'caption='[[3sn2]], [[Resolution|resolution]] 2.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sn2]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SN2 FirstGlance]. <br>
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<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>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ipy|2ipy]], [[3snp|3snp]]</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]] 2.99&#8491;</td></tr>
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<tr><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 Oryctolagus cuniculus])</td></tr>
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<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>
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<tr><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>
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</table>
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<tr><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://www.rcsb.org/pdb/explore.do?structureId=3sn2 RCSB], [http://www.ebi.ac.uk/pdbsum/3sn2 PDBsum]</span></td></tr>
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== Function ==
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<table>
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Iron regulatory protein 1 (IRP1) binds iron-responsive elements (IREs) in messenger RNAs (mRNAs), to repress translation or degradation, or binds an iron-sulfur cluster, to become a cytosolic aconitase enzyme. The 2.8 angstrom resolution crystal structure of the IRP1:ferritin H IRE complex shows an open protein conformation compared with that of cytosolic aconitase. The extended, L-shaped IRP1 molecule embraces the IRE stem-loop through interactions at two sites separated by approximately 30 angstroms, each involving about a dozen protein:RNA bonds. Extensive conformational changes related to binding the IRE or an iron-sulfur cluster explain the alternate functions of IRP1 as an mRNA regulator or enzyme.
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Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA.,Walden WE, Selezneva AI, Dupuy J, Volbeda A, Fontecilla-Camps JC, Theil EC, Volz K Science. 2006 Dec 22;314(5807):1903-8. PMID:17185597<ref>PMID:17185597</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Aconitase 3D structures|Aconitase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aconitate hydratase]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Selezneva, A I.]]
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[[Category: Selezneva AI]]
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[[Category: Volz, K.]]
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[[Category: Volz K]]
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[[Category: Walden, W E.]]
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[[Category: Walden WE]]
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[[Category: Iron sulfur cluster binding]]
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[[Category: Lyase-rna complex]]
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[[Category: Phosphorylation]]
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[[Category: Rna binding]]
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Current revision

Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNA

PDB ID 3sn2

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