3sdp
From Proteopedia
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THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS
Overview
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.
About this Structure
3SDP is a Single protein structure of sequence from Pseudomonas putida with as ligand. The following page contains interesting information on the relation of 3SDP with [Superoxide Dismutase]. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Fri Feb 15 17:44:16 2008
