The MepRAB operon in Staphylococcus aureus has been identified to play a role in drug resistance. Although the functions of MepA and MepR are known, little information is available on the function of MepB. Here we report the X-ray structure of MepB to 2.1 A revealing its structural similarity to the PD-(D/E)XK family of endonucleases. We further show that MepB binds DNA and RNA, with a higher affinity towards RNA and single stranded DNA than towards double stranded DNA. Notably, the PD-(D/E)XK catalytic active site residues are not conserved in MepB. MepB's association with a drug resistance operon suggests that it plays a role in responding to antimicrobials. This role is likely carried out through MepB's interactions with nucleic acids.
Structural characterization of MepB from Staphylococcus aureus reveals homology to endonucleases.,Agah S, Poulos S, Banchs C, Faham S Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2438. PMID:24501097[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Agah S, Poulos S, Banchs C, Faham S. Structural characterization of MepB from Staphylococcus aureus reveals homology to endonucleases. Protein Sci. 2014 Feb 6. doi: 10.1002/pro.2438. PMID:24501097 doi:http://dx.doi.org/10.1002/pro.2438
