3SDP

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

3SDP の概要

• エントリーDOI: 10.2210/pdb3sdp/pdb
• 分子名称: IRON SUPEROXIDE DISMUTASE, FE (III) ION (3 entities in total)
• 機能のキーワード: oxidoreductase (superoxide acceptor)
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43213.58

構造登録者

Stoddard, B.L.,Ringe, D.,Petsko, G.A. (登録日: 1991-05-06, 公開日: 1993-04-15, 最終更新日: 2024-02-28)

主引用文献

Stoddard, B.L.,Howell, P.L.,Ringe, D.,Petsko, G.A.
The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis.
Biochemistry, 29:8885-8893, 1990

PubMed Abstract: 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.

PubMed: 2271564
DOI: 10.1021/bi00490a002

実験手法

X-RAY DIFFRACTION (2.1 Å)