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PDBsum entry 1rw3
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Transferase, replication
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PDB id
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1rw3
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structure of the monomeric reverse transcriptase from moloney murine leukemia virus.
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Authors
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D.Das,
M.M.Georgiadis.
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Ref.
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Structure, 2004,
12,
819-829.
[DOI no: ]
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PubMed id
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Abstract
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Reverse transcriptases (RTs) are multidomain enzymes of variable architecture
that couple both RNA- and DNA-directed DNA polymerase activities with an RNase H
activity specific for an RNA:DNA hybrid in order to replicate the
single-stranded RNA genome of the retrovirus. Previous structural work has been
reported for the heterodimeric HIV-1 and HIV-2 RTs. We now report the first
crystal structure of the full-length Moloney murine leukemia virus (MMLV) RT at
3.0 A resolution. The structure reveals a clamp-shaped molecule resulting from
the relative positions of the thumb, connection, and RNase H domains that is
strikingly different from the HIV-1 RT and provides the first example of a
monomeric reverse transcriptase. A comparative analysis with related DNA
polymerases suggests a unique trajectory for the template-primer exiting the
polymerase active site and provides insights regarding processive DNA synthesis
by MMLV RT.
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Figure 2.
Figure 2. The Crystal Structure of the MMLV RT and a
Comparison with the p66 Subunit of the HIV-1 RT(A) A ribbon
rendering of the MMLV RT is shown with the fingers domain in
red, palm in blue, thumb in green, connection in yellow, and the
RNase H in magenta.(B) A structural comparison of the MMLV RT
monomer is shown in the same color scheme as in (A) with the p66
subunit of HIV-1 RT shown in gray. The structures were
superimposed using the highly conserved structural elements in
the palm domains. In contrast to the rather extended p66 subunit
of HIV-1 RT, the MMLV RT is a far more clamp-shaped molecule.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
819-829)
copyright 2004.
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