2C9V

Atomic resolution structure of Cu-Zn Human Superoxide dismutase

Summary for 2C9V

• Entry DOI: 10.2210/pdb2c9v/pdb
• Related: 1AZV 1BA9 1DSW 1FUN 1HL4 1HL5 1KMG 1L3N 1MFM 1N18 1N19 1OEZ 1OZT 1OZU 1P1V 1PTZ 1PU0 1RK7 1SOS 1SPD 1UXL 1UXM 2AF2 2C9S 2C9U 4SOD
• Descriptor: SUPEROXIDE DISMUTASE [CU-ZN], COPPER (II) ION, ZINC ION, ... (6 entities in total)
• Functional Keywords: oxidoreductase, acetylation, amyotrophic lateral sclerosis, antioxidant, copper, disease mutation, human cu, metal-binding, oxioreductase, zinc, zn superoxide dismutase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: P00441
• Total number of polymer chains: 2
• Total formula weight: 32439.33

Authors

Strange, R.W.,Antonyuk, S.V.,Hough, M.A.,Doucette, P.A.,Valentine, J.S.,Hasnain, S.S. (deposition date: 2005-12-14, release date: 2005-12-20, Last modification date: 2023-12-13)

Primary citation

Strange, R.W.,Antonyuk, S.V.,Hough, M.A.,Doucette, P.A.,Valentine, J.S.,Hasnain, S.S.
Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu-Zn, Zn-Zn and as-Isolated Wild-Type Enzymes.
J.Mol.Biol., 356:1152-, 2006

PubMed Abstract: Human Cu-Zn superoxide dismutase (SOD1) protects cells from the effects of oxidative stress. Mutations in SOD1 are linked to the familial form of amyotrophic lateral sclerosis. Several hypotheses for their toxicity involve the mis-metallation of the enzyme. We present atomic-resolution crystal structures and biophysical data for human SOD1 in three metallation states: Zn-Zn, Cu-Zn and as-isolated. These data represent the first atomic-resolution structures for human SOD1, the first structure of a reduced SOD1, and the first structure of a fully Zn-substituted SOD1 enzyme. Recombinantly expressed as-isolated SOD1 contains a mixture of Zn and Cu at the Cu-binding site. The Zn-Zn structure appears to be at least as stable as the correctly (Cu-Zn) metallated enzyme. These data raise the possibility that in a cellular environment with low availability of free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its interaction with the copper chaperone.

PubMed: 16406071
DOI: 10.1016/J.JMB.2005.11.081

Experimental method

X-RAY DIFFRACTION (1.07 Å)