4B3O

Structures of HIV-1 RT and RNA-DNA Complex Reveal a Unique RT Conformation and Substrate Interface

4B3O の概要

• エントリーDOI: 10.2210/pdb4b3o/pdb
• 関連するPDBエントリー: 1A30 1BV7 1BV9 1BVE 1BVG 1BWA 1BWB 1C0T 1C0U 1C1B 1C1C 1DMP 1DTQ 1DTT 1E6J 1EP4 1ESK 1EX4 1EXQ 1FB7 1FK9 1FKO 1FKP 1G6L 1HIV 1HVH 1HVR 1HWR 1HXB 1JKH 1JLA 1JLB 1JLC 1JLE 1JLF 1JLG 1JLQ 1KLM 1LV1 1LW0 1LW2 1LWC 1LWE 1LWF 1NCP 1O1W 1ODW 1ODY 1QBR 1QBS 1QBT 1QBU 1REV 1RT1 1RT2 1RT3 1RT4 1RT5 1RT6 1RT7 1RTD 1RTH 1RTI 1RTJ 1S1T 1S1U 1S1V 1S1W 1S1X 1T05 1TAM 1TKT 1TKX 1TKZ 1TL1 1TL3 1VRT 1VRU 2WHH 2WOM 2WON 3PHV 4B37 4B3P 4B3Q
• 分子名称: REVERSE TRANSCRIPTASE/RIBONUCLEASE H, P51 RT, 5'-D(*CP*GP*TP*AP*TP*GP*CP*CP*TP*AP*TP*AP*GP*TP *TP*AP*TP*TP*GP*TP*GP*GP*CP*C)-3', ... (6 entities in total)
• 機能のキーワード: hydrolase-dna-rna complex, rnase h, subunit interface, hydrolase/dna/rna
• 由来する生物種: HUMAN IMMUNODEFICIENCY VIRUS 1 (HIV-1); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 132110.62

構造登録者

Lapkouski, M.,Tian, L.,Miller, J.T.,Le Grice, S.F.J.,Yang, W. (登録日: 2012-07-25, 公開日: 2013-01-16, 最終更新日: 2023-12-20)

主引用文献

Lapkouski, M.,Tian, L.,Miller, J.T.,Le Grice, S.F.J.,Yang, W.
Complexes of HIV-1 RT, Nnrti and RNA/DNA Hybrid Reveal a Structure Compatible with RNA Degradation
Nat.Struct.Mol.Biol., 20:230-, 2013

PubMed Abstract: Hundreds of structures of type 1 human immunodeficiency virus (HIV-1) reverse transcriptase (RT) have been determined, but only one contains an RNA/DNA hybrid. Here we report three structures of HIV-1 RT complexed with a non-nucleotide RT inhibitor (NNRTI) and an RNA/DNA hybrid. In the presence of an NNRTI, the RNA/DNA structure differs from all prior nucleic acid-RT structures including the RNA/DNA hybrid. The enzyme structure also differs from all previous RT-DNA complexes. Thus, the hybrid has ready access to the RNase-H active site. These observations indicate that an RT-nucleic acid complex may adopt two structural states, one competent for DNA polymerization and the other for RNA degradation. RT mutations that confer drug resistance but are distant from the inhibitor-binding sites often map to the unique RT-hybrid interface that undergoes conformational changes between two catalytic states.

PubMed: 23314251
DOI: 10.1038/NSMB.2485

実験手法

X-RAY DIFFRACTION (3.3 Å)