3ZK7
CRYSTAL STRUCTURE OF PNEUMOCOCCAL SURFACE ANTIGEN PSAA IN THE METAL-FREE, OPEN STATE
3ZK7 の概要
| エントリーDOI | 10.2210/pdb3zk7/pdb |
| 関連するPDBエントリー | 3ZK8 3ZK9 3ZKA 3ZTT |
| 分子名称 | MANGANESE ABC TRANSPORTER SUBSTRATE-BINDING LIPOPROTEIN, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| 機能のキーワード | metal transport, atp-binding cassette transporters, lipoprotein, membrane transport protein |
| 由来する生物種 | STREPTOCOCCUS PNEUMONIAE (PNEUMOCOCCUS) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 63379.35 |
| 構造登録者 | Counago, R.M.,Ween, M.P.,Bajaj, M.,Zuegg, J.,Cooper, M.A.,McEwan, A.G.,Paton, J.C.,Kobe, B.,McDevitt, C.A. (登録日: 2013-01-22, 公開日: 2013-11-06, 最終更新日: 2023-12-20) |
| 主引用文献 | Counago, R.M.,Ween, M.P.,Begg, S.L.,Bajaj, M.,Zuegg, J.,O'Mara, M.L.,Cooper, M.A.,McEwan, A.G.,Paton, J.C.,Kobe, B.,McDevitt, C.A. Imperfect coordination chemistry facilitates metal ion release in the Psa permease. Nat. Chem. Biol., 10:35-41, 2014 Cited by PubMed Abstract: The relative stability of divalent first-row transition metal ion complexes, as defined by the Irving-Williams series, poses a fundamental chemical challenge for selectivity in bacterial metal ion acquisition. Here we show that although the substrate-binding protein of Streptococcus pneumoniae, PsaA, is finely attuned to bind its physiological substrate manganese, it can also bind a broad range of other divalent transition metal cations. By combining high-resolution structural data, metal-binding assays and mutational analyses, we show that the inability of open-state PsaA to satisfy the preferred coordination chemistry of manganese enables the protein to undergo the conformational changes required for cargo release to the Psa permease. This is specific for manganese ions, whereas zinc ions remain bound to PsaA. Collectively, these findings suggest a new ligand binding and release mechanism for PsaA and related substrate-binding proteins that facilitate specificity for divalent cations during competition from zinc ions, which are more abundant in biological systems. PubMed: 24212134DOI: 10.1038/nchembio.1382 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.69 Å) |
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