2Q32

Crystal structure of human heme oxygenase-2 C127A (HO-2)

Summary for 2Q32

• Entry DOI: 10.2210/pdb2q32/pdb
• Descriptor: Heme oxygenase 2, OXTOXYNOL-10 (3 entities in total)
• Functional Keywords: ho-2, heme oxygenase, structural genomics medical relevance, structural genomics community request, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Microsome: P30519
• Total number of polymer chains: 2
• Total formula weight: 62276.24

Authors

Bianchetti, C.M.,Bingman, C.A.,Bitto, E.,Wesenberg, G.E.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2007-05-29, release date: 2007-06-05, Last modification date: 2023-08-30)

Primary citation

Bianchetti, C.M.,Yi, L.,Ragsdale, S.W.,Phillips Jr., G.N.
Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2.
J.Biol.Chem., 282:37624-37631, 2007

PubMed Abstract: Heme oxygenase (HO) catalyzes the first step in the heme degradation pathway. The crystal structures of apo- and heme-bound truncated human HO-2 reveal a primarily alpha-helical architecture similar to that of human HO-1 and other known HOs. Proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His(45), resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr(154), Lys(199), and Arg(203) orient the heme through direct interactions with the heme propionates. The rearrangements of side chains in heme-bound HO-2 compared with apoHO-2 further elucidate HO-2 heme interactions.

PubMed: 17965015
DOI: 10.1074/jbc.M707396200

Experimental method

X-RAY DIFFRACTION (2.4 Å)