1hrh
From Proteopedia
(New page: 200px<br /> <applet load="1hrh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrh, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1hrh.gif|left|200px]]<br /> | + | [[Image:1hrh.gif|left|200px]]<br /><applet load="1hrh" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hrh" size=" | + | |
caption="1hrh, resolution 2.4Å" /> | caption="1hrh, resolution 2.4Å" /> | ||
'''CRYSTAL STRUCTURE OF THE RIBONUCLEASE H DOMAIN OF HIV-1 REVERSE TRANSCRIPTASE'''<br /> | '''CRYSTAL STRUCTURE OF THE RIBONUCLEASE H DOMAIN OF HIV-1 REVERSE TRANSCRIPTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the ribonuclease (RNase) H domain of HIV-1 | + | The crystal structure of the ribonuclease (RNase) H domain of HIV-1 reverse transcriptase (RT) has been determined at a resolution of 2.4 A and refined to a crystallographic R factor of 0.20. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The overall structure is similar in most respects to the RNase H from Escherichia coli. Structural features characteristic of the retroviral protein suggest how it may interface with the DNA polymerase domain of p66 in the mature RT heterodimer. These features also offer insights into why the isolated RNase H domain is catalytically inactive but when combined in vitro with the isolated p51 domain of RT RNase H activity can be reconstituted. Surprisingly, the peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of p66 is completely inaccessible to solvent in the structure reported here. This suggests that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded. |
==About this Structure== | ==About this Structure== | ||
| - | 1HRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http:// | + | 1HRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: /II, J | + | [[Category: /II, J F.Davies.]] |
| - | [[Category: Matthews, D | + | [[Category: Matthews, D A.]] |
[[Category: hydrolase(endoribonuclease)]] | [[Category: hydrolase(endoribonuclease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:06 2008'' |
Revision as of 11:04, 21 February 2008
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CRYSTAL STRUCTURE OF THE RIBONUCLEASE H DOMAIN OF HIV-1 REVERSE TRANSCRIPTASE
Overview
The crystal structure of the ribonuclease (RNase) H domain of HIV-1 reverse transcriptase (RT) has been determined at a resolution of 2.4 A and refined to a crystallographic R factor of 0.20. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The overall structure is similar in most respects to the RNase H from Escherichia coli. Structural features characteristic of the retroviral protein suggest how it may interface with the DNA polymerase domain of p66 in the mature RT heterodimer. These features also offer insights into why the isolated RNase H domain is catalytically inactive but when combined in vitro with the isolated p51 domain of RT RNase H activity can be reconstituted. Surprisingly, the peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of p66 is completely inaccessible to solvent in the structure reported here. This suggests that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded.
About this Structure
1HRH is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase., Davies JF 2nd, Hostomska Z, Hostomsky Z, Jordan SR, Matthews DA, Science. 1991 Apr 5;252(5002):88-95. PMID:1707186
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