2RSP

STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS SARCOMA RETROVIRUS REFINED AT 2 ANGSTROMS RESOLUTION

2RSP の概要

• エントリーDOI: 10.2210/pdb2rsp/pdb
• 分子名称: RSV PROTEASE (2 entities in total)
• 機能のキーワード: hydrolase(aspartyl proteinase)
• 由来する生物種: Rous sarcoma virus
• 細胞内の位置: Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03322
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27251.72

構造登録者

Wlodawer, A.,Miller, M.,Jaskolski, M. (登録日: 1989-10-17, 公開日: 1989-10-17, 最終更新日: 2024-02-21)

主引用文献

Jaskolski, M.,Miller, M.,Rao, J.K.,Leis, J.,Wlodawer, A.
Structure of the aspartic protease from Rous sarcoma retrovirus refined at 2-A resolution.
Biochemistry, 29:5889-5898, 1990

PubMed Abstract: The structure of Rous sarcoma virus protease has been solved by multiple isomorphous replacement in the crystal form belonging to space group P3(1)21, with unit-cell parameters a = 88.95 A and c = 78.90 A. The enzyme belongs to the family of aspartic proteases with two identical subunits composing the active homodimer. The noncrystallographic dyad relating these two subunits was identified after preliminary tracing in the MIR map and was used for phase improvement by electron-density averaging. Structure refinement resulted in a model that included 1772 protein atoms and 252 water molecules, with an R factor of 0.144 for data extending to 2 A. The secondary structure of a retroviral protease molecule closely resembles that of a single domain in pepsin-like aspartic proteases and consists of several beta-strands and of one well-defined and one distorted alpha-helix. The dimer interface is composed of the N- and C-terminal chains from both subunits which are intertwined to form a well-ordered four-stranded antiparallel beta-sheet. In each monomer, the catalytic triad (Asp-Ser-Gly) is located in a loop that forms a part of the psi-structure characteristic to all aspartic proteases. The position of a water molecule between the active-site aspartate residues and the general scheme of H bonding within the active site bear close resemblance to those in pepsin-like aspartic proteases and therefore suggest a similar enzymatic mechanism. The binding cleft over the active site is covered by two flap arms, one from each monomer, which are partially disordered. The retroviral protease dimer has been compared with several enzymes of cellular origin, with chains aligning to an rms deviation of 1.90 A or better.

PubMed: 2166563
DOI: 10.1021/bi00477a002

実験手法

X-RAY DIFFRACTION (2 Å)