1n6q
From Proteopedia
(New page: 200px<br /> <applet load="1n6q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n6q, resolution 3.Å" /> '''HIV-1 Reverse Transcr...) |
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| - | [[Image:1n6q.gif|left|200px]]<br /> | + | [[Image:1n6q.gif|left|200px]]<br /><applet load="1n6q" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1n6q" size=" | + | |
caption="1n6q, resolution 3.Å" /> | caption="1n6q, resolution 3.Å" /> | ||
'''HIV-1 Reverse Transcriptase Crosslinked to pre-translocation AZTMP-terminated DNA (complex N)'''<br /> | '''HIV-1 Reverse Transcriptase Crosslinked to pre-translocation AZTMP-terminated DNA (complex N)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | AZT (3'-azido-3'-deoxythymidine) resistance involves the enhanced excision | + | AZT (3'-azido-3'-deoxythymidine) resistance involves the enhanced excision of AZTMP from the end of the primer strand by HIV-1 reverse transcriptase. This reaction can occur when an AZTMP-terminated primer is bound at the nucleotide-binding site (pre-translocation complex N) but not at the 'priming' site (post-translocation complex P). We determined the crystal structures of N and P complexes at 3.0 and 3.1 A resolution. These structures provide insight into the structural basis of AZTMP excision and the mechanism of translocation. Docking of a dNTP in the P complex structure suggests steric crowding in forming a stable ternary complex that should increase the relative amount of the N complex, which is the substrate for excision. Structural differences between complexes N and P suggest that the conserved YMDD loop is involved in translocation, acting as a springboard that helps to propel the primer terminus from the N to the P site after dNMP incorporation. |
==About this Structure== | ==About this Structure== | ||
| - | 1N6Q 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] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1N6Q 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] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1N6Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: RNA-directed DNA polymerase]] | [[Category: RNA-directed DNA polymerase]] | ||
[[Category: Arnold, E.]] | [[Category: Arnold, E.]] | ||
| - | [[Category: Birktoft, J | + | [[Category: Birktoft, J J.]] |
| - | [[Category: Boyer, P | + | [[Category: Boyer, P L.]] |
[[Category: Das, K.]] | [[Category: Das, K.]] | ||
| - | [[Category: Hughes, S | + | [[Category: Hughes, S H.]] |
[[Category: Ilankumaran, I.]] | [[Category: Ilankumaran, I.]] | ||
| - | [[Category: Jerina, D | + | [[Category: Jerina, D M.]] |
| - | [[Category: Jr., A | + | [[Category: Jr., A D.Clark.]] |
| - | [[Category: Ramesha, A | + | [[Category: Ramesha, A R.]] |
| - | [[Category: Sarafianos, S | + | [[Category: Sarafianos, S G.]] |
| - | [[Category: Sayer, J | + | [[Category: Sayer, J M.]] |
[[Category: Tuske, S.]] | [[Category: Tuske, S.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: translocation]] | [[Category: translocation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:50 2008'' |
Revision as of 12:02, 21 February 2008
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HIV-1 Reverse Transcriptase Crosslinked to pre-translocation AZTMP-terminated DNA (complex N)
Overview
AZT (3'-azido-3'-deoxythymidine) resistance involves the enhanced excision of AZTMP from the end of the primer strand by HIV-1 reverse transcriptase. This reaction can occur when an AZTMP-terminated primer is bound at the nucleotide-binding site (pre-translocation complex N) but not at the 'priming' site (post-translocation complex P). We determined the crystal structures of N and P complexes at 3.0 and 3.1 A resolution. These structures provide insight into the structural basis of AZTMP excision and the mechanism of translocation. Docking of a dNTP in the P complex structure suggests steric crowding in forming a stable ternary complex that should increase the relative amount of the N complex, which is the substrate for excision. Structural differences between complexes N and P suggest that the conserved YMDD loop is involved in translocation, acting as a springboard that helps to propel the primer terminus from the N to the P site after dNMP incorporation.
About this Structure
1N6Q is a Protein complex structure of sequences from Human immunodeficiency virus 1 and Mus musculus with as ligand. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.
Reference
Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA., Sarafianos SG, Clark AD Jr, Das K, Tuske S, Birktoft JJ, Ilankumaran P, Ramesha AR, Sayer JM, Jerina DM, Boyer PL, Hughes SH, Arnold E, EMBO J. 2002 Dec 2;21(23):6614-24. PMID:12456667
Page seeded by OCA on Thu Feb 21 14:02:50 2008
Categories: Human immunodeficiency virus 1 | Mus musculus | Protein complex | RNA-directed DNA polymerase | Arnold, E. | Birktoft, J J. | Boyer, P L. | Das, K. | Hughes, S H. | Ilankumaran, I. | Jerina, D M. | Jr., A D.Clark. | Ramesha, A R. | Sarafianos, S G. | Sayer, J M. | Tuske, S. | MG | Complex n | Drug resistance | Hiv | Nucleotide excision | Pre-translocation | Reverse transcriptase | Translocation
