2PL2
Crystal structure of TTC0263: a thermophilic TPR protein in Thermus thermophilus HB27
2PL2 の概要
| エントリーDOI | 10.2210/pdb2pl2/pdb |
| 分子名称 | Hypothetical conserved protein TTC0263 (2 entities in total) |
| 機能のキーワード | tpr, protein binding |
| 由来する生物種 | Thermus thermophilus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 48777.79 |
| 構造登録者 | |
| 主引用文献 | Lim, H.,Kim, K.,Han, D.,Oh, J.,Kim, Y. Crystal structure of TTC0263, a thermophilic TPR protein from Thermus thermophilus HB27. Mol.Cell, 24:27-36, 2007 Cited by PubMed Abstract: The hypothetical protein TTC0263 of Thermus thermophilus HB27 is a thermophilic tetratricopeptide repeat (TPR)-containing protein. In the present study, the TPR region (residues 26-230) was resolved at 2.5 A with R-factors of R/Rfree = 23.6%/28.6%. TTC0263 consists of 11 helices that form five TPR units. Uniquely, it contains one atypical "extended" TPR (eTPR) unit. This comprises extended helical residues near the loop region of TTC0263, such that the helical length of eTPR is longer than that of the canonical TPR sequence. In addition, the hybrid TPR domain of TTC0263 possesses oligomer-forming characteristics. TPR domains are generally involved in forming multi-subunit complexes by interacting with each other or with other subunit proteins. The dynamic structure of TTC0263 described here goes some way to explaining how TPR domains mediate the formation of multi-subunit complexes. PubMed: 17846496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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