1XBW

1.9A Crystal Structure of the protein isdG from Staphylococcus aureus aureus, Structural genomics, MCSG

Summary for 1XBW

• Entry DOI: 10.2210/pdb1xbw/pdb
• Related: 1SUE
• Descriptor: hypothetical protein isdG (2 entities in total)
• Functional Keywords: structural genomics, protein structure initiative, mcsg, staphylococcus aureus, protein isdg, psi, midwest center for structural genomics, unknown function
• Biological source: Staphylococcus aureus subsp. aureus
• Cellular location: Cytoplasm (By similarity): Q8NX62
• Total number of polymer chains: 4
• Total formula weight: 51182.03

Authors

Zhang, R.,Wu, R.,Joachimiak, G.,Schneewind, O.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2004-08-31, release date: 2004-10-12, Last modification date: 2024-02-14)

Primary citation

Wu, R.,Skaar, E.P.,Zhang, R.,Joachimiak, G.,Gornicki, P.,Schneewind, O.,Joachimiak, A.
Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases.
J.Biol.Chem., 280:2840-2846, 2005

PubMed Abstract: Heme-degrading enzymes are involved in human diseases ranging from stroke, cancer, and multiple sclerosis to infectious diseases such as malaria, diphtheria, and meningitis. All mammalian and microbial enzymes identified to date are members of the heme oxygenase superfamily and assume similar monomeric structures with an all alpha-helical fold. Here we describe the crystal structures of IsdG and IsdI, two heme-degrading enzymes from Staphylococcus aureus. The structures of both enzymes resemble the ferredoxin-like fold and form a beta-barrel at the dimer interface. Two large pockets found on the outside of the barrel contain the putative active sites. Sequence homologs of IsdG and IsdI were identified in multiple Gram-positive pathogens. Substitution of conserved IsdG amino acid residues either reduced or abolished heme degradation, suggesting a common catalytic mechanism. This mechanism of IsdG-mediated heme degradation may be similar to that of the structurally related monooxygenases, enzymes involved in the synthesis of antibiotics in Streptomyces. Our results imply the evolutionary adaptation of microbial enzymes to unique environments.

PubMed: 15520015
DOI: 10.1074/jbc.M409526200

Experimental method

X-RAY DIFFRACTION (1.9 Å)