1we1

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spinqualitylabelsall models 1we1, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC6803 in complex with heme

Overview

Heme oxygenase (HO) catalyzes the oxidative degradation of heme utilizing, molecular oxygen and reducing equivalents. In photosynthetic organisms, HO, functions in the biosynthesis of such open-chain tetrapyrroles as, phyto-chromobilin and phycobilins, which are involved in the signal, transduction for light responses and light harvesting for photosynthesis, respectively. We have determined the first crystal structure of a HO-1, from a photosynthetic organism, Synechocystis sp. PCC 6803 (Syn HO-1), in, complex with heme at 2.5 A resolution. Heme-Syn HO-1 shares a common, folding with other heme-HOs. Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such, features as the flexibility of the distal helix and hydrophobicity. In, addition, 2-propanol derived from the crystallization solution occupied, the hydrophobic cavity, which is proposed to be a CO trapping site in rat, HO-1 that suppresses product inhibition. Although Syn HO-1 and mammalian, HO-1 are similar in overall structure and amino acid sequence (57%, similarity vs. human HO-1), their molecular surfaces differ in charge, distribution. The surfaces of the heme binding sides are both positively, charged, but this patch of Syn HO-1 is narrow compared to that of, mammalian HO-1. This feature is suited to the selective binding of, ferredoxin, the physiological redox partner of Syn HO-1; the molecular, size of ferredoxin is approximately 10 kDa whereas the size of, NADPH-cytochrome P450 reductase, a reducing partner of mammalian HO-1, is, approximately 77 kDa. A docking model of heme-Syn HO-1 and ferredoxin, suggests indirect electron transfer from an iron-sulfur cluster in, ferredoxin to the heme iron of heme-Syn HO-1.

About this Structure

1WE1 is a Single protein structure of sequence from Synechocystis sp. with PO4, CL, HEM and IPA as ligands. Active as Heme oxygenase, with EC number 1.14.99.3 Full crystallographic information is available from OCA.

Reference

Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme., Sugishima M, Migita CT, Zhang X, Yoshida T, Fukuyama K, Eur J Biochem. 2004 Nov;271(22):4517-25. PMID:15560792

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