1EK0
GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION
1EK0 の概要
エントリーDOI | 10.2210/pdb1ek0/pdb |
分子名称 | PROTEIN (GTP-BINDING PROTEIN YPT51), MAGNESIUM ION, NICKEL (II) ION, ... (6 entities in total) |
機能のキーワード | g protein, vesicular traffic, gtp hydrolysis, ypt/rab protein, endocytosis, hydrolase, endocytosis-exocytosis complex, endocytosis/exocytosis |
由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
細胞内の位置 | Endosome membrane ; Lipid- anchor : P36017 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 20012.06 |
構造登録者 | |
主引用文献 | Esters, H.,Alexandrov, K.,Constantinescu, A.T.,Goody, R.S.,Scheidig, A.J. High-resolution crystal structure of S. cerevisiae Ypt51(DeltaC15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis. J.Mol.Biol., 298:111-121, 2000 Cited by PubMed Abstract: Ypt/Rab proteins are membrane-associated small GTP-binding proteins which play a central role in the coordination, activation and regulation of vesicle-mediated transport in eukaryotic cells. We present the 1.5 A high-resolution crystal structure of Ypt51 in its active, GppNHp-bound conformation. Ypt51 is an important regulator involved in the endocytic membrane traffic of Saccharomyces cerevisiae. The structure reveals small but significant structural differences compared with H-Ras p21. The effector loop and the catalytic loop are well defined and stabilized by extensive hydrophobic interactions. The switch I and switch II regions form a well-defined epitope for hypothetical effector protein binding. Sequence comparisons between the different isoforms Ypt51, Ypt52 and Ypt53 provide the first insights into determinants for specific effector binding and for fine-tuning of the intrinsic GTP-hydrolysis rate. PubMed: 10756108DOI: 10.1006/jmbi.2000.3645 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.48 Å) |
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