5Y8B の概要
| エントリーDOI | 10.2210/pdb5y8b/pdb |
| 関連するPDBエントリー | 5GIZ 5GJ3 5Y89 5Y8A |
| 分子名称 | Periplasmic binding protein, MAGNESIUM ION (3 entities in total) |
| 機能のキーワード | metal transport, transport protein |
| 由来する生物種 | Roseiflexus sp. (strain RS-1) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 28294.93 |
| 構造登録者 | Rahman, M.M.,Naoe, Y.,Nakamura, N.,Doi, A.,Shiro, Y.,Sugimoto, H. (登録日: 2017-08-20, 公開日: 2017-10-11, 最終更新日: 2023-11-22) |
| 主引用文献 | Naoe, Y.,Nakamura, N.,Rahman, M.M.,Tosha, T.,Nagatoishi, S.,Tsumoto, K.,Shiro, Y.,Sugimoto, H. Structural basis for binding and transfer of heme in bacterial heme-acquisition systems Proteins, 85:2217-2230, 2017 Cited by PubMed Abstract: Periplasmic heme-binding proteins (PBPs) in Gram-negative bacteria are components of the heme acquisition system. These proteins shuttle heme across the periplasmic space from outer membrane receptors to ATP-binding cassette (ABC) heme importers located in the inner-membrane. In the present study, we characterized the structures of PBPs found in the pathogen Burkholderia cenocepacia (BhuT) and in the thermophile Roseiflexus sp. RS-1 (RhuT) in the heme-free and heme-bound forms. The conserved motif, in which a well-conserved Tyr interacts with the nearby Arg coordinates on heme iron, was observed in both PBPs. The heme was recognized by its surroundings in a variety of manners including hydrophobic interactions and hydrogen bonds, which was confirmed by isothermal titration calorimetry. Furthermore, this study of 3 forms of BhuT allowed the first structural comparison and showed that the heme-binding cleft of BhuT adopts an "open" state in the heme-free and 2-heme-bound forms, and a "closed" state in the one-heme-bound form with unique conformational changes. Such a conformational change might adjust the interaction of the heme(s) with the residues in PBP and facilitate the transfer of the heme into the translocation channel of the importer. PubMed: 28913898DOI: 10.1002/prot.25386 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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