2BPI

Structure of Iron dependent superoxide dismutase from P. falciparum.

Summary for 2BPI

• Entry DOI: 10.2210/pdb2bpi/pdb
• Descriptor: FE-SUPEROXIDE DISMUTASE, FE (III) ION (3 entities in total)
• Functional Keywords: dismutase, oxidoreductase, metal-binding
• Biological source: PLASMODIUM FALCIPARUM
• Total number of polymer chains: 2
• Total formula weight: 47775.17

Authors

Boucher, I.W.,Brannigan, J.,Wilkinson, A.J.,Brzozowski, M. (deposition date: 2005-04-20, release date: 2006-10-11, Last modification date: 2023-12-13)

Primary citation

Boucher, I.W.,Brzozowski, A.M.,Brannigan, J.A.,Schnick, C.,Smith, D.J.,Kyes, S.A.,Wilkinson, A.J.
The Crystal Structure of Superoxide Dismutase from Plasmodium Falciparum.
Bmc Struct.Biol., 6:20-, 2006

PubMed Abstract: Superoxide dismutases (SODs) are important enzymes in defence against oxidative stress. In Plasmodium falciparum, they may be expected to have special significance since part of the parasite life cycle is spent in red blood cells where the formation of reactive oxygen species is likely to be promoted by the products of haemoglobin breakdown. Thus, inhibitors of P. falciparum SODs have potential as anti-malarial compounds. As a step towards their development we have determined the crystal structure of the parasite's cytosolic iron superoxide dismutase.

PubMed: 17020617
DOI: 10.1186/1472-6807-6-20

Experimental method

X-RAY DIFFRACTION (2.52 Å)