1TOA
PERIPLASMIC ZINC BINDING PROTEIN TROA FROM TREPONEMA PALLIDUM
1TOA の概要
| エントリーDOI | 10.2210/pdb1toa/pdb |
| 分子名称 | PROTEIN (PERIPLASMIC BINDING PROTEIN TROA), ZINC ION, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | periplasmic binding protein, zinc binding protein, abc transporter, binding protein |
| 由来する生物種 | Treponema pallidum |
| 細胞内の位置 | Periplasm: P96116 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 69246.77 |
| 構造登録者 | Lee, Y.H.,Deka, R.K.,Norgard, M.V.,Radolf, J.D.,Hasemann, C.A. (登録日: 1999-03-03, 公開日: 1999-07-05, 最終更新日: 2023-12-27) |
| 主引用文献 | Lee, Y.H.,Deka, R.K.,Norgard, M.V.,Radolf, J.D.,Hasemann, C.A. Treponema pallidum TroA is a periplasmic zinc-binding protein with a helical backbone. Nat.Struct.Biol., 6:628-633, 1999 Cited by PubMed Abstract: The crystal structure of recombinant TroA, a zinc-binding protein component of an ATP-binding cassette transport system in Treponema pallidum, was determined at a resolution of 1.8 A. The organization of the protein is largely similar to other periplasmic ligand-binding proteins (PLBP), in that two independent globular domains interact with each other to create a zinc-binding cleft between them. The structure has one bound zinc pentavalently coordinated to residues from both domains. Unlike previous PLBP structures that have an interdomain hinge composed of beta-strands, the N- and C-domains of TroA are linked by a single long backbone helix. This unique backbone helical conformation was possibly adopted to limit the hinge motion associated with ligand exchange. PubMed: 10404217DOI: 10.1038/10677 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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