2atf: Difference between revisions

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[[Image:2atf.png|left|200px]]


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==X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056==
The line below this paragraph, containing "STRUCTURE_2atf", creates the "Structure Box" on the page.
<StructureSection load='2atf' size='340' side='right'caption='[[2atf]], [[Resolution|resolution]] 1.75&Aring;' 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'>[[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>
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]] 1.75&#8491;</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
{{STRUCTURE_2atf|  PDB=2atf  |  SCENE=  }}
<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>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_16492780}}, adds the Publication Abstract to the page
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16492780 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_16492780}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2ATF is a 1 chain 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].
 
==Reference==
<ref group="xtra">PMID:16492780</ref><references group="xtra"/>
[[Category: Cysteine dioxygenase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Allard, S T.M.]]
[[Category: Allard STM]]
[[Category: Bingman, C A.]]
[[Category: Bingman CA]]
[[Category: Bitto, E.]]
[[Category: Bitto E]]
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
[[Category: Mccoy JG]]
[[Category: Jr., G N.Phillips.]]
[[Category: Phillips Jr GN]]
[[Category: Mccoy, J G.]]
[[Category: Wesenberg GE]]
[[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 Tue Feb 17 06:20:06 2009''

Latest revision as of 10:50, 30 October 2024

X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056X-RAY STRUCTURE OF cysteine dioxygenase type I FROM MUS MUSCULUS MM.241056

Structural highlights

2atf is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

CDO1_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr. Structure and mechanism of mouse cysteine dioxygenase. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. PMID:16492780

2atf, resolution 1.75Å

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