1SOS

ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE

Summary for 1SOS

• Entry DOI: 10.2210/pdb1sos/pdb
• Descriptor: SUPEROXIDE DISMUTASE, COPPER (II) ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase (superoxide acceptor)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P00441
• Total number of polymer chains: 10
• Total formula weight: 159536.36

Authors

Parge, H.E.,Hallewell, R.A.,Tainer, J.A. (deposition date: 1992-02-11, release date: 1993-04-15, Last modification date: 2024-11-06)

Primary citation

Parge, H.E.,Hallewell, R.A.,Tainer, J.A.
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.
Proc.Natl.Acad.Sci.USA, 89:6109-6113, 1992

PubMed Abstract: Superoxide dismutase enzymes protect aerobic organisms from oxygen-mediated free-radical damage. Crystallographic structures of recombinant human Cu,Zn superoxide dismutase have been determined, refined, and analyzed at 2.5 A resolution for wild-type and a designed thermostable double-mutant enzyme (Cys-6----Ala, Cys-111----Ser). The 10 subunits (five dimers) in the crystallographic asymmetric unit form an unusual stable open lattice with 80-A-diameter channels. The 10 independently fit and refined subunits provide high accuracy, error analysis, and insights on loop conformations. There is a helix dipole interaction with the Zn site, and 14 residues form two or more structurally conserved side-chain to main-chain hydrogen bonds that appear critical to active-site architecture, loop conformation, and the increased stability resulting from the Cys-111----Ser mutation.

PubMed: 1463506
DOI: 10.1073/pnas.89.13.6109

Experimental method

X-RAY DIFFRACTION (2.5 Å)