2aps: Difference between revisions
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|PDB= 2aps |SIZE=350|CAPTION= <scene name='initialview01'>2aps</scene>, resolution 1.9Å | |PDB= 2aps |SIZE=350|CAPTION= <scene name='initialview01'>2aps</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SODC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=715 Actinobacillus pleuropneumoniae]) | |GENE= SODC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=715 Actinobacillus pleuropneumoniae]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aps OCA], [http://www.ebi.ac.uk/pdbsum/2aps PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2aps RCSB]</span> | |||
}} | }} | ||
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[[Category: Kroll, J S.]] | [[Category: Kroll, J S.]] | ||
[[Category: Langford, P R.]] | [[Category: Langford, P R.]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: sod]] | [[Category: sod]] | ||
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[[Category: water-mediated dimer]] | [[Category: water-mediated dimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:55:40 2008'' | ||
Revision as of 01:55, 31 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SODC (Actinobacillus pleuropneumoniae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CU/ZN SUPEROXIDE DISMUTASE FROM ACTINOBACILLUS PLEUROPNEUMONIAE
OverviewOverview
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 StructureAbout this Structure
2APS is a Single protein structure of sequence from Actinobacillus pleuropneumoniae. Full crystallographic information is available from OCA.
ReferenceReference
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
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