3sn2

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[[Image:3sn2.jpg|left|200px]]
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==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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== 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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</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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<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><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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<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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<table>
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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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The line below this paragraph, containing "STRUCTURE_3sn2", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3sn2| PDB=3sn2 | SCENE= }}
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===Crystal structure analysis of iron regulatory protein 1 in complex with transferrin receptor IRE B RNA===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_17185597}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 17185597 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_17185597}}
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==About this Structure==
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[[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].
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==Reference==
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<ref group="xtra">PMID:017185597</ref><references group="xtra"/>
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[[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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