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2b5h

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[[Image:2b5h.gif|left|200px]]
 
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{{Structure
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==1.5 A Resolution Crystal Structure of Recombinant R. Norvegicus Cysteine Dioxygenase==
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|PDB= 2b5h |SIZE=350|CAPTION= <scene name='initialview01'>2b5h</scene>, resolution 1.50&Aring;
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<StructureSection load='2b5h' size='340' side='right'caption='[[2b5h]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene>
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<table><tr><td colspan='2'>[[2b5h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5H FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cysteine_dioxygenase Cysteine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.20 1.13.11.20]
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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]] 1.5&#8491;</td></tr>
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|GENE= Cdo1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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}}
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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=2b5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5h OCA], [https://pdbe.org/2b5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5h RCSB], [https://www.ebi.ac.uk/pdbsum/2b5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDO1_RAT CDO1_RAT]
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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/b5/2b5h_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=2b5h ConSurf].
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<div style="clear:both"></div>
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'''1.5 A Resolution Crystal Structure of Recombinant R. Norvegicus Cysteine Dioxygenase'''
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==See Also==
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Cysteine dioxygenase is a mononuclear iron-dependent enzyme responsible for the oxidation of cysteine with molecular oxygen to form cysteine sulfinate. This reaction commits cysteine to either catabolism to sulfate and pyruvate or the taurine biosynthetic pathway. Cysteine dioxygenase is a member of the cupin superfamily of proteins. The crystal structure of recombinant rat cysteine dioxygenase has been determined to 1.5-A resolution, and these results confirm the canonical cupin beta-sandwich fold and the rare cysteinyltyrosine intramolecular cross-link (between Cys(93) and Tyr(157)) seen in the recently reported murine cysteine dioxygenase structure. In contrast to the catalytically inactive mononuclear Ni(II) metallocenter present in the murine structure, crystallization of a catalytically competent preparation of rat cysteine dioxygenase revealed a novel tetrahedrally coordinated mononuclear iron center involving three histidines (His(86), His(88), and His(140)) and a water molecule. Attempts to acquire a structure with bound ligand using either cocrystallization or soaking crystals with cysteine revealed the formation of a mixed disulfide involving Cys(164) near the active site, which may explain previously observed substrate inhibition. This work provides a framework for understanding the molecular mechanisms involved in thiol dioxygenation and sets the stage for exploration of the chemistry of both the novel mononuclear iron center and the catalytic role of the cysteinyl-tyrosine linkage.
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[[Category: Large Structures]]
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==About this Structure==
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2B5H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5H OCA].
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==Reference==
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Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation., Simmons CR, Liu Q, Huang Q, Hao Q, Begley TP, Karplus PA, Stipanuk MH, J Biol Chem. 2006 Jul 7;281(27):18723-33. Epub 2006 Apr 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16611640 16611640]
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[[Category: Cysteine dioxygenase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Begley TP]]
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[[Category: Begley, T P.]]
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[[Category: Hao Q]]
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[[Category: Hao, Q.]]
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[[Category: Huang Q]]
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[[Category: Huang, Q.]]
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[[Category: Karplus PA]]
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[[Category: Karplus, P A.]]
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[[Category: Liu Q]]
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[[Category: Liu, Q.]]
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[[Category: Simmons CR]]
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[[Category: Simmons, C R.]]
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[[Category: Stipanuk MH]]
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[[Category: Stipanuk, M H.]]
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[[Category: FE]]
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[[Category: beta-sandwich]]
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[[Category: cupin fold]]
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[[Category: jelly-roll topology]]
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[[Category: tetrahedral iron coordination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:49 2008''
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Current revision

1.5 A Resolution Crystal Structure of Recombinant R. Norvegicus Cysteine Dioxygenase

PDB ID 2b5h

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