The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.

ABSTRACT:

Background

The ribonuclease H (RNase H) domains of retroviral reverse transcriptases play an essential role in the replication cycle of retroviruses. During reverse transcription of the viral genomic RNA, an RNA/DNA hybrid is created whose RNA strand needs to be hydrolyzed by the RNase H to enable synthesis of the second DNA strand by the DNA polymerase function of the reverse transcriptase. Here, we report the solution structure of the separately purified RNase H domain from prototype foamy virus (PFV) revealing the so-called C-helix and the adjacent basic loop, which both were suggested to be important in substrate binding and activity.

Results

The solution structure of PFV RNase H shows that it contains a mixed five-stranded β-sheet, which is sandwiched by four α-helices

SUBMITTER: Leo B 

PROVIDER: S-EPMC3443672 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature