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PDBsum entry 1hys

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Top Page protein dna_rna Protein-protein interface(s) links
Transferase/DNA-RNA hybrid PDB id
1hys
Contents
Protein chains
553 a.a. *
425 a.a. *
214 a.a. *
220 a.a. *
DNA/RNA
* Residue conservation analysis

References listed in PDB file
Key reference
Title Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA.
Authors S.G.Sarafianos, K.Das, C.Tantillo, A.D.Clark, J.Ding, J.M.Whitcomb, P.L.Boyer, S.H.Hughes, E.Arnold.
Ref. EMBO J, 2001, 20, 1449-1461. [DOI no: 10.1093/emboj/20.6.1449]
PubMed id 11250910
Abstract
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.
Figure 3.
Figure 3 Stereo view of a ribbon representation of the structure of HIV-1 RT in complex with the polypurine RNA:DNA. The fingers, palm, thumb, connection and RNase H subdomains of p66 are colored blue, red, green, yellow and orange, respectively. The p51 subunit is colored gray. The RNA template and DNA primer strands are shown in magenta and blue, respectively.
Figure 5.
Figure 5 Simulated annealing (F[o] - F[c]) omit electron density maps contoured at the 2 level at the polymerase active site (1) (omitting nucleic acid) and of the unpaired residue of template (2) (omitting unpaired residue Tem-15-Ade).
The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2001, 20, 1449-1461) copyright 2001.
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