Crystal structure of human heme oxygenase-1
| Autor: | D J, Schuller, A, Wilks, P R, Ortiz de Montellano, T L, Poulos |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Protein Folding Binding Sites Protein Conformation Iron Molecular Sequence Data Static Electricity Glycine Membrane Proteins Heme Crystallography X-Ray Ligands Peptide Fragments Protein Structure Secondary Substrate Specificity Oxygen Heme Oxygenase (Decyclizing) Solvents Humans Histidine Pliability Heme Oxygenase-1 |
| Zdroj: | Nature structural biology. 6(9) |
| ISSN: | 1072-8368 |
| Popis: | Heme oxygenase catalyzes the first step in the oxidative degradation of heme. The crystal structure of heme oxygenase-1 (HO-1) reported here reveals a novel helical fold with the heme sandwiched between two helices. The proximal helix provides a heme iron ligand, His 25. Conserved glycines in the distal helix near the oxygen binding site allow close contact between the helix backbone and heme in addition to providing flexibility for substrate binding and product release. Regioselective oxygenation of the alpha-meso heme carbon is due primarily to steric influence of the distal helix. |
| Databáze: | OpenAIRE |
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