2C4B
Inhibitor cystine knot protein McoEeTI fused to the catalytically inactive barnase mutant H102A
2C4B の概要
| エントリーDOI | 10.2210/pdb2c4b/pdb |
| 分子名称 | BARNASE MCOEETI FUSION, NONAETHYLENE GLYCOL, GLYCEROL, ... (9 entities in total) |
| 機能のキーワード | squash inhibitor, hybrid microprotein, fusion protein, ribonuclease, endonuclease, hydrolase, nuclease, protease inhibitor, serine protease inhibitor |
| 由来する生物種 | BACILLUS AMYLOLIQUEFACIENS 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 35792.51 |
| 構造登録者 | Niemann, H.H.,Schmoldt, H.U.,Wentzel, A.,Kolmar, H.,Heinz, D.W. (登録日: 2005-10-18, 公開日: 2005-11-21, 最終更新日: 2024-10-23) |
| 主引用文献 | Niemann, H.H.,Schmoldt, H.U.,Wentzel, A.,Kolmar, H.,Heinz, D.W. Barnase Fusion as a Tool to Determine the Crystal Structure of the Small Disulfide-Rich Protein Mcoeeti. J.Mol.Biol., 356:1-, 2006 Cited by PubMed Abstract: We present a fusion system suited to determine the crystal structure of small disulfide-rich proteins. McoEeTI, a hybrid inhibitor cystine knot microprotein, was produced as a soluble fusion to a catalytically inactive variant of the RNAse barnase in Escherichia coli. Functioning as a versatile tag, barnase facilitated purification, crystallization and high-resolution structure determination. Flexibility of the linker region allows for different relative orientations of barnase and the fusion partner in two crystallographically independent molecules and may thereby facilitate crystal packing. Nevertheless, the linker region is well ordered in both molecules. This system may prove more generally useful to determine the crystal structure of peptides and small proteins. PubMed: 16337652DOI: 10.1016/J.JMB.2005.11.005 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.3 Å) |
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