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| - | {{Seed}} | |
| - | [[Image:2b3x.png|left|200px]] | |
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| - | <!-- | + | ==Structure of an orthorhombic crystal form of human cytosolic aconitase (IRP1)== |
| - | The line below this paragraph, containing "STRUCTURE_2b3x", creates the "Structure Box" on the page.
| + | <StructureSection load='2b3x' size='340' side='right'caption='[[2b3x]], [[Resolution|resolution]] 2.54Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2b3x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B3X FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54Å</td></tr> |
| - | -->
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | {{STRUCTURE_2b3x| PDB=2b3x | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b3x OCA], [https://pdbe.org/2b3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b3x RCSB], [https://www.ebi.ac.uk/pdbsum/2b3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b3x ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ACOHC_HUMAN ACOHC_HUMAN] Bifunctional iron sensor that switches between 2 activities depending on iron availability (PubMed:1946430, PubMed:1281544, PubMed:8041788). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization (PubMed:1946430, PubMed:1281544, PubMed:8041788, PubMed:23891004). 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:1946430, PubMed:1281544, PubMed:8041788, PubMed:23891004).<ref>PMID:1281544</ref> <ref>PMID:1946430</ref> <ref>PMID:23891004</ref> <ref>PMID:8041788</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.<ref>PMID:1281544</ref> <ref>PMID:1946430</ref> <ref>PMID:8041788</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/2b3x_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b3x ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | ===Structure of an orthorhombic crystal form of human cytosolic aconitase (IRP1)=== | + | ==See Also== |
| - | | + | *[[Aconitase 3D structures|Aconitase 3D structures]] |
| - | | + | == References == |
| - | <!--
| + | <references/> |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_16407072}}, adds the Publication Abstract to the page
| + | __TOC__ |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 16407072 is the PubMed ID number.
| + | </StructureSection> |
| - | -->
| + | |
| - | {{ABSTRACT_PUBMED_16407072}}
| + | |
| - | | + | |
| - | ==About this Structure==
| + | |
| - | 2B3X is a [[Single protein]] structure of 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=2B3X OCA].
| + | |
| - | | + | |
| - | ==Reference== | + | |
| - | Crystal structure of human iron regulatory protein 1 as cytosolic aconitase., Dupuy J, Volbeda A, Carpentier P, Darnault C, Moulis JM, Fontecilla-Camps JC, Structure. 2006 Jan;14(1):129-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16407072 16407072]
| + | |
| - | [[Category: Aconitate hydratase]]
| + | |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Pdbx_ordinal=, <PDBx:audit_author.]] | + | [[Category: Dupuy J]] |
| - | [[Category: Irp1 ire-irp1 aconitase activity]] | + | [[Category: Fontecilla-Camps JC]] |
| - | [[Category: Lyase]] | + | [[Category: Volbeda A]] |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 25 21:07:00 2009''
| + | |
| Structural highlights
Function
ACOHC_HUMAN Bifunctional iron sensor that switches between 2 activities depending on iron availability (PubMed:1946430, PubMed:1281544, PubMed:8041788). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization (PubMed:1946430, PubMed:1281544, PubMed:8041788, PubMed:23891004). 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:1946430, PubMed:1281544, PubMed:8041788, PubMed:23891004).[1] [2] [3] [4] 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.[5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Haile DJ, Rouault TA, Harford JB, Kennedy MC, Blondin GA, Beinert H, Klausner RD. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11735-9. PMID:1281544 doi:10.1073/pnas.89.24.11735
- ↑ Kaptain S, Downey WE, Tang C, Philpott C, Haile D, Orloff DG, Harford JB, Rouault TA, Klausner RD. A regulated RNA binding protein also possesses aconitase activity. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10109-13. PMID:1946430
- ↑ Stehling O, Mascarenhas J, Vashisht AA, Sheftel AD, Niggemeyer B, Rösser R, Pierik AJ, Wohlschlegel JA, Lill R. Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and maturation of different subsets of cytosolic-nuclear iron-sulfur proteins. Cell Metab. 2013 Aug 6;18(2):187-98. PMID:23891004 doi:10.1016/j.cmet.2013.06.015
- ↑ Philpott CC, Klausner RD, Rouault TA. The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7321-5. PMID:8041788
- ↑ Haile DJ, Rouault TA, Harford JB, Kennedy MC, Blondin GA, Beinert H, Klausner RD. Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11735-9. PMID:1281544 doi:10.1073/pnas.89.24.11735
- ↑ Kaptain S, Downey WE, Tang C, Philpott C, Haile D, Orloff DG, Harford JB, Rouault TA, Klausner RD. A regulated RNA binding protein also possesses aconitase activity. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10109-13. PMID:1946430
- ↑ Philpott CC, Klausner RD, Rouault TA. The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7321-5. PMID:8041788
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