3LGN

Crystal structure of IsdI in complex with heme

Summary for 3LGN

• Entry DOI: 10.2210/pdb3lgn/pdb
• Related: 3LGM
• Descriptor: Heme-degrading monooxygenase isdI, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
• Functional Keywords: dimeric alpha+beta barrel, cytoplasm, heme, iron, metal-binding, monooxygenase, oxidoreductase
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm (By similarity): Q7A827
• Total number of polymer chains: 2
• Total formula weight: 27352.06

Authors

Ukpabi, G.N.,Murphy, M.E.P. (deposition date: 2010-01-20, release date: 2010-03-09, Last modification date: 2023-11-01)

Primary citation

Reniere, M.L.,Ukpabi, G.N.,Harry, S.R.,Stec, D.F.,Krull, R.,Wright, D.W.,Bachmann, B.O.,Murphy, M.E.P.,Skaar, E.P.
The IsdG-family of haem oxygenases degrades haem to a novel chromophore
Mol.Microbiol., 75:1529-1538, 2010

PubMed Abstract: Enzymatic haem catabolism by haem oxygenases is conserved from bacteria to humans and proceeds through a common mechanism leading to the formation of iron, carbon monoxide and biliverdin. The first members of a novel class of haem oxygenases were recently identified in Staphylococcus aureus (IsdG and IsdI) and were termed the IsdG-family of haem oxygenases. Enzymes of the IsdG-family form tertiary structures distinct from those of the canonical haem oxygenase family, suggesting that IsdG-family members degrade haem via a unique reaction mechanism. Herein we report that the IsdG-family of haem oxygenases degrade haem to the oxo-bilirubin chromophore staphylobilin. We also present the crystal structure of haem-bound IsdI in which haem ruffling and constrained binding of oxygen is consistent with cleavage of the porphyrin ring at the beta- or delta-meso carbons. Combined, these data establish that the IsdG-family of haem oxygenases degrades haem to a novel chromophore distinct from biliverdin.

PubMed: 20180905
DOI: 10.1111/j.1365-2958.2010.07076.x

Experimental method

X-RAY DIFFRACTION (1.5 Å)