1YU6
Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex
1YU6 の概要
| エントリーDOI | 10.2210/pdb1yu6/pdb |
| 分子名称 | Subtilisin Carlsberg, Ovomucoid, CALCIUM ION, ... (4 entities in total) |
| 機能のキーワード | protein proteinase inhibitor, protease, hydrolase |
| 由来する生物種 | Meleagris gallopavo (turkey) 詳細 |
| 細胞内の位置 | Secreted: P00780 P68390 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 95310.08 |
| 構造登録者 | Maynes, J.T.,Cherney, M.M.,Qasim, M.A.,Laskowski Jr., M.,James, M.N.G. (登録日: 2005-02-11, 公開日: 2005-05-03, 最終更新日: 2024-11-13) |
| 主引用文献 | Maynes, J.T.,Cherney, M.M.,Qasim, M.A.,Laskowski Jr, M.,James, M.N. Structure of the subtilisin Carlsberg-OMTKY3 complex reveals two different ovomucoid conformations. Acta Crystallogr.,Sect.D, 61:580-588, 2005 Cited by PubMed Abstract: One of the most studied protein proteinase inhibitors is the turkey ovomucoid third domain, OMTKY3. This inhibitor contains a reactive-site loop (Lys13I-Arg21I) that binds in a nearly identical manner to all studied serine proteinases, regardless of their clan or specificity. The crystal structure of OMTKY3 bound to subtilisin Carlsberg (CARL) has been determined. There are two complete copies of the complexes in the crystallographic asymmetric unit. Whereas the two enzyme molecules are virtually identical [0.16 A root-mean-square difference (r.m.s.d.) for 274 C(alpha) atoms], the two inhibitor molecules show dramatic differences between one another (r.m.s.d. = 2.4 A for 50 C(alpha) atoms). When compared with other proteinase-bound OMTKY3 molecules, these inhibitors show even larger differences. This work facilitates a re-evaluation of the importance of certain ovomucoid residues in proteinase binding and explains why additivity and sequence-based binding-prediction methods fail for the CARL-OMTKY3 complex. PubMed: 15858268DOI: 10.1107/S0907444905004889 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.55 Å) |
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