3sdp

THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS

spinqualitylabelsall models 3sdp, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sdp is a 2 chain structure with sequence from Pseudomonas putida. The October 2007 RCSB PDB Molecule of the Month feature on Superoxide Dismutase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE Activity: Superoxide dismutase, with EC number 1.15.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum Function [SODF_PSEPU] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. 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 The 2.1-A resolution crystal structure of native uncomplexed iron superoxide dismutase (EC 1.15.1.1) from Pseudomonas ovalis was solved and refined to a final R factor of 24%. The dimeric structure contains one catalytic iron center per monomer with an asymmetric trigonal-bipyramidal coordination of protein ligands to the metal. Each monomer contains two domains, with the trigonal ligands (histidines 74 and 160; aspartate 156) contributed by the large domain and stabilized by an extended hydrogen-bonded network, including residues from opposing monomers. The axial ligand (histidine 26) is found on the small domain and does not participate extensively in the stabilizing H-bond network. The open axial coordination position of the iron is devoid of bound water molecules or anions. The metal is located 0.5 A out of the plane of the trigonal ligands toward histidine 26, providing a slightly skewed coordination away from the iron binding site. The molecule contains a glutamine residue in the active site which is conserved between all iron enzymes sequenced to data but which is conserved among all manganese SODs at a separate position in the sequence. This residue shows the same structural interactions in both cases, implying that iron and manganese SODs are second-site revertants of one another. The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis.,Stoddard BL, Howell PL, Ringe D, Petsko GA Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:2271564 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Superoxide Dismutase

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