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[[Image:2q2l.jpg|left|200px]]


{{Structure
==Crystal Structure of Superoxide Dismutase from P. atrosanguina==
|PDB= 2q2l |SIZE=350|CAPTION= <scene name='initialview01'>2q2l</scene>, resolution 2.367&Aring;
<StructureSection load='2q2l' size='340' side='right'caption='[[2q2l]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+1001'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+B+1002'>AC2</scene>, <scene name='pdbsite=AC3:Iod+Binding+Site+For+Residue+A+2003'>AC3</scene>, <scene name='pdbsite=AC4:Iod+Binding+Site+For+Residue+B+2006'>AC4</scene> and <scene name='pdbsite=AC5:Iod+Binding+Site+For+Residue+B+2009'>AC5</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[2q2l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Potentilla_atrosanguinea Potentilla atrosanguinea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q2L FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.367&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00305 Cu-Zn_Superoxide_Dismutase]</span>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q2l OCA], [https://pdbe.org/2q2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q2l RCSB], [https://www.ebi.ac.uk/pdbsum/2q2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q2l ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q2l OCA], [http://www.ebi.ac.uk/pdbsum/2q2l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q2l RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/B2CP37_9ROSA B2CP37_9ROSA] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000393]
== 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/q2/2q2l_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=2q2l ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Superoxide dismutase (SOD) from Potentilla atrosanguinea (Wall. ex. Lehm.) was crystallized using 20% PEG 3350 and 0.2 M ammonium iodide and diffraction data were collected to 2.36 A resolution using an in-house Cu Kalpha X-ray source. Analyses show that data with a redundancy of 3.2 were sufficient to determine the structure by the SAD technique using the iodine anomalous signal. This redundancy is lower than that in previous cases in which protein structures were determined using iodines for phasing and in-house copper X-ray sources. Cocrystallization of proteins with halide salts such as ammonium iodide in combination with copper-anode X-ray radiation can therefore serve as a powerful and easy avenue for structure solution.


'''Crystal Structure of Superoxide Dismutase from P. atrosanguina'''
SAD phasing of a structure based on cocrystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution.,Yogavel M, Gill J, Mishra PC, Sharma A Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):931-4. Epub 2007, Jul 17. PMID:17642520<ref>PMID:17642520</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2q2l" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Superoxide dismutase (SOD) from Potentilla atrosanguinea (Wall. ex. Lehm.) was crystallized using 20% PEG 3350 and 0.2 M ammonium iodide and diffraction data were collected to 2.36 A resolution using an in-house Cu Kalpha X-ray source. Analyses show that data with a redundancy of 3.2 were sufficient to determine the structure by the SAD technique using the iodine anomalous signal. This redundancy is lower than that in previous cases in which protein structures were determined using iodines for phasing and in-house copper X-ray sources. Cocrystallization of proteins with halide salts such as ammonium iodide in combination with copper-anode X-ray radiation can therefore serve as a powerful and easy avenue for structure solution.
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2Q2L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Potentilla_atrosanguinea Potentilla atrosanguinea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q2L OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
SAD phasing of a structure based on cocrystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution., Yogavel M, Gill J, Mishra PC, Sharma A, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):931-4. Epub 2007, Jul 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17642520 17642520]
[[Category: Potentilla atrosanguinea]]
[[Category: Potentilla atrosanguinea]]
[[Category: Protein complex]]
[[Category: Gill J]]
[[Category: Superoxide dismutase]]
[[Category: Manickam Y]]
[[Category: Gill, J.]]
[[Category: Mishra PC]]
[[Category: Manickam, Y.]]
[[Category: Sharma A]]
[[Category: Mishra, P C.]]
[[Category: Sharma, A.]]
[[Category: antioxidant]]
[[Category: metal-binding]]
[[Category: oxidoreductase]]
[[Category: sad]]
[[Category: sod]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:43:43 2008''

Latest revision as of 08:31, 30 October 2024

Crystal Structure of Superoxide Dismutase from P. atrosanguina

2q2l, resolution 2.37Å

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