3NZ3
Crystal structure of the mucin-binding domain of Spr1345 from Streptococcus pneumoniae
3NZ3 の概要
| エントリーDOI | 10.2210/pdb3nz3/pdb |
| 分子名称 | Putative uncharacterized protein, TRIETHYLENE GLYCOL, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | all beta sheets, ig-like fold, mucin-binding, mucin, cell surface, cell adhesion |
| 由来する生物種 | Streptococcus pneumoniae |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12984.33 |
| 構造登録者 | Du, Y.,He, Y.-X.,Zhang, Z.-Y.,Yang, Y.-H.,Shi, W.-W.,Frolet, C.,Guilmi, A.M.,Vernet, T.,Zhou, C.-Z.,Chen, Y. (登録日: 2010-07-15, 公開日: 2011-04-20, 最終更新日: 2024-03-20) |
| 主引用文献 | Du, Y.,He, Y.-X.,Zhang, Z.-Y.,Yang, Y.-H.,Shi, W.-W.,Frolet, C.,Guilmi, A.M.,Vernet, T.,Zhou, C.-Z.,Chen, Y. Crystal structure of the mucin-binding domain of Spr1345 from Streptococcus pneumoniae J.Struct.Biol., 174:252-257, 2011 Cited by PubMed Abstract: The surface protein Spr1345 from Streptococcus pneumoniae R6 is a 22-kDa mucin-binding protein (MucBP) involved in adherence and colonization of the human lung and respiratory tract. It is composed of a mucin-binding domain (MucBD) and a proline-rich domain (PRD) followed by an LPxTG motif, which is recognized and cleaved by sortase, resulting in a mature form of 171 residues (MF171) that is anchored to the cell wall. We found that the MucBD alone possesses comparable in vitro mucin-binding affinity to the mature form, and can be specifically enriched at the surface of human lung carcinoma A549 cells. Using single-wavelength anomalous dispersion (SAD) phasing method with the iodine signals, we solved the crystal structure of the MucBD at 2.0Å resolution, the first structure of MucBDs from pathogenic bacteria. The overall structure adopts an immunoglobulin-like fold with an elongated rod-like shape, composed of six anti-parallel β-strands and a long loop. Structural comparison suggested that the conserved C-terminal moiety may participate in the recognition of mucins. These findings provided structural insights into host-pathogen interaction mediated by mucins, which might be useful for designing novel vaccines and antibiotic drugs against human diseases caused by pneumococci. PubMed: 21055474DOI: 10.1016/j.jsb.2010.10.016 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






