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[[Image:2aps.gif|left|200px]]
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{{STRUCTURE_2aps|  PDB=2aps  |  SCENE=  }}
'''CU/ZN SUPEROXIDE DISMUTASE FROM ACTINOBACILLUS PLEUROPNEUMONIAE'''


==CU/ZN SUPEROXIDE DISMUTASE FROM ACTINOBACILLUS PLEUROPNEUMONIAE==
<StructureSection load='2aps' size='340' side='right'caption='[[2aps]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2aps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinobacillus_pleuropneumoniae Actinobacillus pleuropneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2APS 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aps OCA], [https://pdbe.org/2aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aps RCSB], [https://www.ebi.ac.uk/pdbsum/2aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aps ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SODC_ACTPL SODC_ACTPL] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
== 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/ap/2aps_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=2aps ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Macrophages and neutrophils protect animals from microbial infection in part by issuing a burst of toxic superoxide radicals when challenged. To counteract this onslaught, many Gram-negative bacterial pathogens possess periplasmic Cu,Zn superoxide dismutases (SODs), which act on superoxide to yield molecular oxygen and hydrogen peroxide. We have solved the X-ray crystal structure of the Cu,Zn SOD from Actinobacillus pleuropneumoniae, a major porcine pathogen, by molecular replacement at 1.9 A resolution. The structure reveals that the dimeric bacterial enzymes form a structurally homologous class defined by a water-mediated dimer interface, and share with all Cu,Zn SODs the Greek-key beta-barrel subunit fold with copper and zinc ions located at the base of a deep loop-enclosed active-site channel. Our structure-based sequence alignment of the bacterial enzymes explains the monomeric nature of at least two of these, and suggests that there may be at least one additional structural class for the bacterial SODs. Two metal-mediated crystal contacts yielded our C222(1) crystals, and the geometry of these sites could be engineered into proteins recalcitrant to crystallization in their native form. This work highlights structural differences between eukaryotic and prokaryotic Cu,Zn SODs, as well as similarities and differences among prokaryotic SODs, and lays the groundwork for development of antimicrobial drugs that specifically target periplasmic Cu,Zn SODs of bacterial pathogens.


==Overview==
Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface.,Forest KT, Langford PR, Kroll JS, Getzoff ED J Mol Biol. 2000 Feb 11;296(1):145-53. PMID:10656823<ref>PMID:10656823</ref>
Macrophages and neutrophils protect animals from microbial infection in part by issuing a burst of toxic superoxide radicals when challenged. To counteract this onslaught, many Gram-negative bacterial pathogens possess periplasmic Cu,Zn superoxide dismutases (SODs), which act on superoxide to yield molecular oxygen and hydrogen peroxide. We have solved the X-ray crystal structure of the Cu,Zn SOD from Actinobacillus pleuropneumoniae, a major porcine pathogen, by molecular replacement at 1.9 A resolution. The structure reveals that the dimeric bacterial enzymes form a structurally homologous class defined by a water-mediated dimer interface, and share with all Cu,Zn SODs the Greek-key beta-barrel subunit fold with copper and zinc ions located at the base of a deep loop-enclosed active-site channel. Our structure-based sequence alignment of the bacterial enzymes explains the monomeric nature of at least two of these, and suggests that there may be at least one additional structural class for the bacterial SODs. Two metal-mediated crystal contacts yielded our C222(1) crystals, and the geometry of these sites could be engineered into proteins recalcitrant to crystallization in their native form. This work highlights structural differences between eukaryotic and prokaryotic Cu,Zn SODs, as well as similarities and differences among prokaryotic SODs, and lays the groundwork for development of antimicrobial drugs that specifically target periplasmic Cu,Zn SODs of bacterial pathogens.


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


==Reference==
==See Also==
Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface., Forest KT, Langford PR, Kroll JS, Getzoff ED, J Mol Biol. 2000 Feb 11;296(1):145-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10656823 10656823]
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinobacillus pleuropneumoniae]]
[[Category: Actinobacillus pleuropneumoniae]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Forest, K T.]]
[[Category: Forest KT]]
[[Category: Getzoff, E D.]]
[[Category: Getzoff ED]]
[[Category: Kroll, J S.]]
[[Category: Kroll JS]]
[[Category: Langford, P R.]]
[[Category: Langford PR]]
[[Category: Beta barrel]]
[[Category: Sod]]
[[Category: Superoxide dismutase]]
[[Category: Water-mediated dimer]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:19:36 2008''
Retrieved from "https://proteopedia.org/2aps"