2hji

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[[Image:2hji.png|left|200px]]
 
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==Structural model for the Fe-containing isoform of acireductone dioxygenase==
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The line below this paragraph, containing "STRUCTURE_2hji", creates the "Structure Box" on the page.
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<StructureSection load='2hji' size='340' side='right'caption='[[2hji]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2hji]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HJI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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{{STRUCTURE_2hji| PDB=2hji | SCENE= }}
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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=2hji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hji OCA], [https://pdbe.org/2hji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hji RCSB], [https://www.ebi.ac.uk/pdbsum/2hji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hji ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MTND_KLEOX MTND_KLEOX] Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.<ref>PMID:8407993</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hj/2hji_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2hji ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acireductone dioxygenase (ARD) catalyzes different reactions between O2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene (acireductone) depending upon the metal bound in the active site. Ni2+ -ARD cleaves acireductone to formate, CO and methylthiopropionate. If Fe2+ is bound (ARD'), the same substrates yield methylthioketobutyrate and formate. The two forms differ in structure, and are chromatographically separable. Paramagnetism of Fe2+ renders the active site of ARD' inaccessible to standard NMR methods. The structure of ARD' has been determined using Fe2+ binding parameters determined by X-ray absorption spectroscopy and NMR restraints from H98S ARD, a metal-free diamagnetic protein that is isostructural with ARD'. ARD' retains the beta-sandwich fold of ARD, but a structural entropy switch increases order at one end of a two-helix system that bisects the beta-sandwich and decreases order at the other upon interconversion of ARD and ARD', causing loss of the C-terminal helix in ARD' and rearrangements of residues involved in substrate orientation in the active site.
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===Structural model for the Fe-containing isoform of acireductone dioxygenase===
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One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase.,Ju T, Goldsmith RB, Chai SC, Maroney MJ, Pochapsky SS, Pochapsky TC J Mol Biol. 2006 Nov 3;363(4):823-34. Epub 2006 Aug 26. PMID:16989860<ref>PMID:16989860</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16989860}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2hji" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16989860 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16989860}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2hji]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJI OCA].
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==Reference==
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<ref group="xtra">PMID:16989860</ref><ref group="xtra">PMID:9880484</ref><references group="xtra"/>
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[[Category: Klebsiella oxytoca]]
[[Category: Klebsiella oxytoca]]
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[[Category: Chai, S C.]]
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[[Category: Large Structures]]
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[[Category: Ju, T.]]
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[[Category: Chai SC]]
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[[Category: Maroney, M J.]]
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[[Category: Ju T]]
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[[Category: Pochapsky, T C.]]
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[[Category: Maroney MJ]]
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[[Category: Dioxygenase]]
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[[Category: Pochapsky TC]]
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[[Category: Isozyme]]
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[[Category: Methionine salvage]]
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[[Category: Non-heme iron]]
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[[Category: Oxidoreductase]]
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[[Category: Structural entropy]]
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Current revision

Structural model for the Fe-containing isoform of acireductone dioxygenase

PDB ID 2hji

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