2atf: Difference between revisions

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-[[Image:2atf.gif|left|200px]]
- {{Structure
+==X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056==
-|PDB= 2atf |SIZE=350|CAPTION= <scene name='initialview01'>2atf</scene>, resolution 1.75&Aring;
+<StructureSection load='2atf' size='340' side='right'caption='[[2atf]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
+<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>
-|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]
+</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>
-|GENE= Cdo1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
+<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.
-'''X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2atf" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-ATF 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].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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]
-[[Category: Cysteine dioxygenase]]
 [[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: EDO]]
-[[Category: NI]]
-[[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 Thu Mar 20 15:53:38 2008''