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[[Image:3sn2.jpg|left|200px]]
==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=''>
== Structural highlights ==
<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>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ipy|2ipy]], [[3snp|3snp]]</td></tr>
<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>
<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>
<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>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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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{{STRUCTURE_3sn2|  PDB=3sn2  |  SCENE=  }}


===Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNA===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
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{{ABSTRACT_PUBMED_17185597}}
 
==About this Structure==
[[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].
 
==Reference==
<ref group="xtra">PMID:017185597</ref><references group="xtra"/>
[[Category: Aconitate hydratase]]
[[Category: Aconitate hydratase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]

Revision as of 05:26, 5 June 2014

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

3sn2, resolution 2.99Å

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