1hys

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spinqualitylabelsall models 1hys, resolution 3.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH A POLYPURINE TRACT RNA:DNA

Overview

We have determined the 3.0 A resolution structure of wild-type HIV-1, reverse transcriptase in complex with an RNA:DNA oligonucleotide whose, sequence includes a purine-rich segment from the HIV-1 genome called the, polypurine tract (PPT). The PPT is resistant to ribonuclease H (RNase H), cleavage and is used as a primer for second DNA strand synthesis. The, 'RNase H primer grip', consisting of amino acids that interact with the, DNA primer strand, may contribute to RNase H catalysis and cleavage, specificity. Cleavage specificity is also controlled by the width of the, minor groove and the trajectory of the RNA:DNA, both of which are sequence, dependent. An unusual 'unzipping' of 7 bp occurs in the adenine stretch of, the PPT: an unpaired base on the template strand takes the base pairing, out of register and then, following two offset base pairs, an unpaired, base on the primer strand re-establishes the normal register. The, structural aberration extends to the RNase H active site and may play a, role in the resistance of PPT to RNase H cleavage.

About this Structure

1HYS is a Protein complex structure of sequences from Human immunodeficiency virus 1 and Mus musculus. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.

Reference

Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA., Sarafianos SG, Das K, Tantillo C, Clark AD Jr, Ding J, Whitcomb JM, Boyer PL, Hughes SH, Arnold E, EMBO J. 2001 Mar 15;20(6):1449-61. PMID:11250910

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