5XC3
Crystal structure of Acanthamoeba polyphaga mimivirus Rab GTPase in complex with GDP
5XC3 の概要
エントリーDOI | 10.2210/pdb5xc3/pdb |
関連するPDBエントリー | 5XC5 |
分子名称 | Probable Rab-related GTPase, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
機能のキーワード | rab gtpase, acanthamoeba polyphaga mimivirus, vesicle trafficking, protein transport |
由来する生物種 | Acanthamoeba polyphaga mimivirus (APMV) |
細胞内の位置 | Host cell membrane ; Lipid- anchor ; Cytoplasmic side : Q5UQ27 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 20677.46 |
構造登録者 | |
主引用文献 | Ku, B.,You, J.A.,Oh, K.J.,Yun, H.Y.,Lee, H.S.,Shin, H.C.,Jung, J.,Shin, Y.B.,Kim, S.J. Crystal structures of two forms of the Acanthamoeba polyphaga mimivirus Rab GTPase Arch. Virol., 162:3407-3416, 2017 Cited by PubMed Abstract: Acanthamoeba polyphaga mimivirus (APMV) is a member of the family of giant viruses, harboring a 1,200 kbp genome within its 700 nm-diameter viral particle. The R214 gene of the APMV genome was recently shown to encode a homologue of the Rab GTPases, molecular switch proteins known to play a pivotal role in the regulation of membrane trafficking that were considered to exist only in eukaryotes. Herein, we report the first crystal structures of GDP- and GTP-bound forms of APMV Rab GTPase, both of which were determined at high resolution. An in-depth structural comparison of APMV Rab with each other and with mammalian Rab homologues led to an atomic-level elucidation of the inactive-active conformational change upon GDP/GTP exchange. APMV Rab GTPase exhibited considerable structural similarity to human Rab5, as previously predicted based on its amino acid sequence. However, it also contains unique structural features differentiating it from mammalian homologues, such as the functional substitution of a phenylalanine residue for the stabilization of the nucleotide's guanine base. PubMed: 28779233DOI: 10.1007/s00705-017-3510-2 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.497 Å) |
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