2qpp

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spinqualitylabelsall models 2qpp, resolution 2.610Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2QPP is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Heme oxygenase, with EC number 1.14.99.3 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2., Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. PMID:17965015

Page seeded by OCA on Wed Jan 23 10:43:53 2008