2W1Z
ROP2 from Toxoplasma gondii: A virulence factor with a protein- kinase fold and no enzymatic activity.
2W1Z の概要
| エントリーDOI | 10.2210/pdb2w1z/pdb |
| 分子名称 | ROP2, SULFATE ION (3 entities in total) |
| 機能のキーワード | inactivity, protein-kinase, membrane-attachment, transferase |
| 由来する生物種 | TOXOPLASMA GONDII |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 85619.55 |
| 構造登録者 | Labesse, G.,Gelin, M.,Bessin, Y.,Lebrun, M.,Arold, S.T.,Dubremetz, J.-F. (登録日: 2008-10-21, 公開日: 2008-12-09, 最終更新日: 2024-10-23) |
| 主引用文献 | Labesse, G.,Gelin, M.,Bessin, Y.,Lebrun, M.,Papoin, J.,Cerdan, R.,Arold, S.T.,Dubremetz, J.-F. Rop2 from Toxoplasma Gondii: A Virulence Factor with a Protein-Kinase Fold and No Enzymatic Activity. Structure, 17:139-, 2009 Cited by PubMed Abstract: The ROP2 protein and its paralogs are important virulence factors secreted into the host cell by the parasite Toxoplasma gondii. Here we describe the crystal structure of a large and soluble domain of mature ROP2, representative of the ROP2-like protein family. This is a structure of a protein-kinase fold that is devoid of catalytic residues and does not bind ATP. Various structural extensions constitute a signature of this protein family and act to maintain the protein kinase in an open conformation. Our ROP2 structure rules out a previous structural model of attachment of ROP2-like proteins to the parasitophorous vacuole membrane. We propose an alternative mode of membrane attachment implicating basic and amphiphatic helices present in the flexible N terminus of ROP2. PubMed: 19141290DOI: 10.1016/J.STR.2008.11.005 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.97 Å) |
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