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1E5D

RUBREDOXIN OXYGEN:OXIDOREDUCTASE (ROO) FROM ANAEROBE DESULFOVIBRIO GIGAS

Summary for 1E5D
Entry DOI10.2210/pdb1e5d/pdb
DescriptorRUBREDOXIN\:OXYGEN OXIDOREDUCTASE, FLAVIN MONONUCLEOTIDE, MU-OXO-DIIRON, ... (5 entities in total)
Functional Keywordsoxidoreductase, oxygenreductase, diiron-centre, flavoproteins, lactamase-fold
Biological sourceDESULFOVIBRIO GIGAS
Total number of polymer chains2
Total formula weight90930.52
Authors
Primary citationFrazao, C.,Silva, G.,Gomes, C.M.,Matias, P.,Coelho, R.,Sieker, L.,Macedo, S.,Liu, M.Y.,Oliveira, S.,Teixeira, M.,Xavier, A.V.,Rodrigues-Pousada, C.,Carrondo, M.A.,Le Gall, J.
Structure of a Dioxygen Reduction Enzyme from Desulfovibrio Gigas
Nat.Struct.Biol., 7:1041-, 2000
Cited by
PubMed Abstract: Desulfovibrio gigas is a strict anaerobe that contains a well-characterized metabolic pathway that enables it to survive transient contacts with oxygen. The terminal enzyme in this pathway, rubredoxin:oxygen oxidoreductase (ROO) reduces oxygen to water in a direct and safe way. The 2.5 A resolution crystal structure of ROO shows that each monomer of this homodimeric enzyme consists of a novel combination of two domains, a flavodoxin-like domain and a Zn-beta-lactamase-like domain that contains a di-iron center for dioxygen reduction. This is the first structure of a member of a superfamily of enzymes widespread in strict and facultative anaerobes, indicating its broad physiological significance.
PubMed: 11062560
DOI: 10.1038/80961
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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