1hys

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(New page: 200px<br /> <applet load="1hys" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hys, resolution 3.0&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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'''CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH A POLYPURINE TRACT RNA:DNA'''<br />
'''CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN COMPLEX WITH A POLYPURINE TRACT RNA:DNA'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1HYS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HYS OCA].
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1HYS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYS OCA].
==Reference==
==Reference==
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[[Category: RNA-directed DNA polymerase]]
[[Category: RNA-directed DNA polymerase]]
[[Category: Arnold, E.]]
[[Category: Arnold, E.]]
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[[Category: Boyer, P.L.]]
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[[Category: Boyer, P L.]]
[[Category: Das, K.]]
[[Category: Das, K.]]
[[Category: Ding, J.]]
[[Category: Ding, J.]]
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[[Category: Hughes, S.H.]]
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[[Category: Hughes, S H.]]
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[[Category: Jr., A.D.Clark.]]
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[[Category: Jr., A D.Clark.]]
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[[Category: Sarafianos, S.G.]]
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[[Category: Sarafianos, S G.]]
[[Category: Tantillo, C.]]
[[Category: Tantillo, C.]]
[[Category: Whitcomb, J.]]
[[Category: Whitcomb, J.]]
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[[Category: unpaired base]]
[[Category: unpaired base]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:09:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:17 2008''

Revision as of 11:06, 21 February 2008


1hys, resolution 3.0Å

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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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