7KSE

Crystal structure of Prototype Foamy Virus Protease-Reverse Transcriptase CSH mutant (selenomethionine-labeled)

7KSE の概要

• エントリーDOI: 10.2210/pdb7kse/pdb
• 分子名称: Peptidase A9/Reverse transcriptase/RNase H, CALCIUM ION (3 entities in total)
• 機能のキーワード: aspartyl protease, hydrolase, multifunctional enzyme, transferase, reverse transcription, viral maturation, viral protein
• 由来する生物種: Eastern chimpanzee simian foamy virus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85825.74

構造登録者

Harrison, J.J.E.K.,Das, K.,Ruiz, F.X.,Arnold, E. (登録日: 2020-11-21, 公開日: 2021-08-11, 最終更新日: 2024-11-06)

主引用文献

Harrison, J.J.E.K.,Tuske, S.,Das, K.,Ruiz, F.X.,Bauman, J.D.,Boyer, P.L.,DeStefano, J.J.,Hughes, S.H.,Arnold, E.
Crystal Structure of a Retroviral Polyprotein: Prototype Foamy Virus Protease-Reverse Transcriptase (PR-RT).
Viruses, 13:-, 2021

PubMed Abstract: In most cases, proteolytic processing of the retroviral Pol portion of the Gag-Pol polyprotein precursor produces protease (PR), reverse transcriptase (RT), and integrase (IN). However, foamy viruses (FVs) express Pol separately from Gag and, when Pol is processed, only the IN domain is released. Here, we report a 2.9 Å resolution crystal structure of the mature PR-RT from prototype FV (PFV) that can carry out both proteolytic processing and reverse transcription but is in a configuration not competent for proteolytic or polymerase activity. PFV PR-RT is monomeric and the architecture of PFV PR is similar to one of the subunits of HIV-1 PR, which is a dimer. There is a C-terminal extension of PFV PR (101-145) that consists of two helices which are adjacent to the base of the RT palm subdomain, and anchors PR to RT. The polymerase domain of PFV RT consists of fingers, palm, thumb, and connection subdomains whose spatial arrangements are similar to the p51 subunit of HIV-1 RT. The RNase H and polymerase domains of PFV RT are connected by flexible linkers. Significant spatial and conformational (sub)domain rearrangements are therefore required for nucleic acid binding. The structure of PFV PR-RT provides insights into the conformational maturation of retroviral Pol polyproteins.

PubMed: 34452360
DOI: 10.3390/v13081495

実験手法

X-RAY DIFFRACTION (3 Å)