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[[Image:2atf.gif|left|200px]]
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{{STRUCTURE_2atf|  PDB=2atf  |  SCENE=  }}
'''X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056'''


==X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056==
<StructureSection load='2atf' size='340' side='right'caption='[[2atf]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2atf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ATF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ATF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2atf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2atf OCA], [https://pdbe.org/2atf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2atf RCSB], [https://www.ebi.ac.uk/pdbsum/2atf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2atf ProSAT], [https://www.topsan.org/Proteins/CESG/2atf TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDO1_MOUSE CDO1_MOUSE]
== 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/at/2atf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2atf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked to autoimmune diseases and neurological disorders. The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms. The sequence is 91% identical to that of a human homolog. The structure reveals that CDO adopts the typical beta-barrel fold of the cupin superfamily. The NE2 atoms of His-86, -88, and -140 provide the metal binding site. The structure further revealed a covalent linkage between the side chains of Cys-93 and Tyr-157, the cysteine of which is conserved only in eukaryotic proteins. Metal analysis showed that the recombinant enzyme contained a mixture of iron, nickel, and zinc, with increased iron content associated with increased catalytic activity. Details of the predicted active site are used to present and discuss a plausible mechanism of action for the enzyme.


==Overview==
Structure and mechanism of mouse cysteine dioxygenase.,McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. PMID:16492780<ref>PMID:16492780</ref>
Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked to autoimmune diseases and neurological disorders. The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms. The sequence is 91% identical to that of a human homolog. The structure reveals that CDO adopts the typical beta-barrel fold of the cupin superfamily. The NE2 atoms of His-86, -88, and -140 provide the metal binding site. The structure further revealed a covalent linkage between the side chains of Cys-93 and Tyr-157, the cysteine of which is conserved only in eukaryotic proteins. Metal analysis showed that the recombinant enzyme contained a mixture of iron, nickel, and zinc, with increased iron content associated with increased catalytic activity. Details of the predicted active site are used to present and discuss a plausible mechanism of action for the enzyme.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2ATF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ATF OCA].
</div>
<div class="pdbe-citations 2atf" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure and mechanism of mouse cysteine dioxygenase., McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr, Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16492780 16492780]
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
[[Category: Cysteine dioxygenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Allard STM]]
[[Category: Allard, S T.M.]]
[[Category: Bingman CA]]
[[Category: Bingman, C A.]]
[[Category: Bitto E]]
[[Category: Bitto, E.]]
[[Category: Mccoy JG]]
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
[[Category: Phillips Jr GN]]
[[Category: Jr., G N.Phillips.]]
[[Category: Wesenberg GE]]
[[Category: Mccoy, J G.]]
[[Category: Wesenberg, G E.]]
[[Category: Bc013638]]
[[Category: Center for eukaryotic structural genomic]]
[[Category: Cesg]]
[[Category: Cupin family]]
[[Category: Mm 241056]]
[[Category: Pfam05995 2 cdo_i]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:27:13 2008''
Retrieved from "https://proteopedia.org/2atf"