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1rw3
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(New page: 200px<br /><applet load="1rw3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rw3, resolution 3.0Å" /> '''The crystal structure...)
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Revision as of 23:46, 20 November 2007
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The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus
Overview
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.
About this Structure
1RW3 is a Single protein structure of sequence from Moloney murine leukemia virus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus., Das D, Georgiadis MM, Structure. 2004 May;12(5):819-29. PMID:15130474
Page seeded by OCA on Wed Nov 21 01:54:02 2007
