6A2J
Crystal structure of heme A synthase from Bacillus subtilis
6A2J の概要
| エントリーDOI | 10.2210/pdb6a2j/pdb |
| 関連するPDBエントリー | 6IED |
| 分子名称 | Heme A synthase, PROTOPORPHYRIN IX CONTAINING FE, COPPER (II) ION, ... (6 entities in total) |
| 機能のキーワード | oxidoreductase, heam biosynthesis, membrane protein |
| 由来する生物種 | Bacillus subtilis (strain 168) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 42921.73 |
| 構造登録者 | Niwa, S.,Takeda, K.,Kosugi, M.,Tsutsumi, E.,Miki, K. (登録日: 2018-06-12, 公開日: 2018-11-21, 最終更新日: 2024-10-30) |
| 主引用文献 | Niwa, S.,Takeda, K.,Kosugi, M.,Tsutsumi, E.,Mogi, T.,Miki, K. Crystal structure of heme A synthase fromBacillus subtilis. Proc. Natl. Acad. Sci. U.S.A., 115:11953-11957, 2018 Cited by PubMed Abstract: Heme A is an essential cofactor for respiratory terminal oxidases and vital for respiration in aerobic organisms. The final step of heme A biosynthesis is formylation of the C-8 methyl group of heme molecule by heme A synthase (HAS). HAS is a heme-containing integral membrane protein, and its structure and reaction mechanisms have remained unknown. Thus, little is known about HAS despite of its importance. Here we report the crystal structure of HAS from at 2.2-Å resolution. The N- and C-terminal halves of HAS consist of four-helix bundles and they align in a pseudo twofold symmetry manner. Each bundle contains a pair of histidine residues and forms a heme-binding domain. The C-half domain binds a cofactor-heme molecule, while the N-half domain is vacant. Many water molecules are found in the transmembrane region and around the substrate-binding site, and some of them interact with the main chain of transmembrane helix. Comparison of these two domain structures enables us to construct a substrate-heme binding state structure. This structure implies that a completely conserved glutamate, Glu57 in , is the catalytic residue for the formylation reaction. These results provide valuable suggestions of the substrate-heme binding mechanism. Our results present significant insight into the heme A biosynthesis. PubMed: 30397130DOI: 10.1073/pnas.1813346115 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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