4AM9
CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION CHAPERONE SYCD IN COMPLEX WITH A PEPTIDE OF THE TRANSLOCATOR YOPD
4AM9 の概要
| エントリーDOI | 10.2210/pdb4am9/pdb |
| 関連するPDBエントリー | 2VGX 2VGY |
| 分子名称 | CHAPERONE SYCD, YOP EFFECTOR YOPD, SULFATE ION, ... (5 entities in total) |
| 機能のキーワード | chaperone, chaperone binding domain, chaperone peptide complex, pathogenictiy factor, translocator, tetratricopeptide repeat, tpr, t3ss, virulence factor |
| 由来する生物種 | YERSINIA ENTEROCOLITICA 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 18204.79 |
| 構造登録者 | |
| 主引用文献 | Schreiner, M.,Niemann, H.H. Crystal Structure of the Yersinia Enterocolitica Type III Secretion Chaperone Sycd in Complex with a Peptide of the Minor Translocator Yopd Bmc Struct.Biol., 12:12-, 2012 Cited by PubMed Abstract: Type III secretion systems are used by Gram-negative bacteria as "macromolecular syringes" to inject effector proteins into eukaryotic cells. Two hydrophobic proteins called translocators form the necessary pore in the host cell membrane. Both translocators depend on binding to a single chaperone in the bacterial cytoplasm to ensure their stability and efficient transport through the secretion needle. It was suggested that the conserved chaperones bind the more divergent translocators via a hexapeptide motif that is found in both translocators and conserved between species. PubMed: 22708907DOI: 10.1186/1472-6807-12-13 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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