An inactivated nuclease-like domain in RecC with novel function: implications for evolution.

ABSTRACT:

Background

The PD-(D/E)xK superfamily, containing a wide variety of other exo- and endonucleases, is a notable example of general function conservation in the face of extreme sequence and structural variation. Almost all members employ a small number of shared conserved residues to bind catalytically essential metal ions and thereby effect DNA cleavage. The crystal structure of the RecBCD prokaryotic DNA repair machinery shows that RecB contains such a nuclease domain at its C-terminus. The RecC C-terminal region was reported as having a novel fold.

Results

The RecC C-terminal region can be divided into an alpha/beta domain and a smaller alpha-helical bundle domain. Here we show that the alpha/beta domain is homologous to the RecB nuclease domain but lacks the features neces

SUBMITTER: Rigden DJ 

PROVIDER: S-EPMC1185551 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature