4LQE

Crystal Structure of MepB

Summary for 4LQE

• Entry DOI: 10.2210/pdb4lqe/pdb
• Descriptor: MepB, SULFATE ION (3 entities in total)
• Functional Keywords: endonuclease, dna binding protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 19355.00

Authors

Faham, S.,Agah, S. (deposition date: 2013-07-17, release date: 2014-03-12, Last modification date: 2014-05-07)

Primary citation

Agah, S.,Poulos, S.,Banchs, C.,Faham, S.
Structural characterization of MepB from Staphylococcus aureus reveals homology to endonucleases.
Protein Sci., 23:594-602, 2014

PubMed Abstract: 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 Å 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.

PubMed: 24501097
DOI: 10.1002/pro.2438

Experimental method

X-RAY DIFFRACTION (2.1 Å)