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-Structure paper
タイトル | Structure of the L Protein of Vesicular Stomatitis Virus from Electron Cryomicroscopy. |
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ジャーナル・号・ページ | Cell, Vol. 162, Issue 2, Page 314-327, Year 2015 |
掲載日 | 2015年7月16日 |
著者 | Bo Liang / Zongli Li / Simon Jenni / Amal A Rahmeh / Benjamin M Morin / Timothy Grant / Nikolaus Grigorieff / Stephen C Harrison / Sean P J Whelan / |
PubMed 要旨 | The large (L) proteins of non-segmented, negative-strand RNA viruses, a group that includes Ebola and rabies viruses, catalyze RNA-dependent RNA polymerization with viral ribonucleoprotein as ...The large (L) proteins of non-segmented, negative-strand RNA viruses, a group that includes Ebola and rabies viruses, catalyze RNA-dependent RNA polymerization with viral ribonucleoprotein as template, a non-canonical sequence of capping and methylation reactions, and polyadenylation of viral messages. We have determined by electron cryomicroscopy the structure of the vesicular stomatitis virus (VSV) L protein. The density map, at a resolution of 3.8 Å, has led to an atomic model for nearly all of the 2109-residue polypeptide chain, which comprises three enzymatic domains (RNA-dependent RNA polymerase [RdRp], polyribonucleotidyl transferase [PRNTase], and methyltransferase) and two structural domains. The RdRp resembles the corresponding enzymatic regions of dsRNA virus polymerases and influenza virus polymerase. A loop from the PRNTase (capping) domain projects into the catalytic site of the RdRp, where it appears to have the role of a priming loop and to couple product elongation to large-scale conformational changes in L. |
リンク | Cell / PubMed:26144317 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.8 Å |
構造データ | |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | TRANSFERASE (転移酵素) / RNA-DEPENDENT RNA POLYMERASE (RNA依存性RNAポリメラーゼ) / RNA CAPPING (5'キャップ) / CRYOEM SINGLE- PARTICLE ANALYSIS |