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4KDP

TcaR-ssDNA complex crystal structure reveals the novel ssDNA binding mechanism of the MarR family proteins

Summary for 4KDP
Entry DOI10.2210/pdb4kdp/pdb
DescriptorTcaR transcription regulator, DNA (5'-D(*CP*GP*CP*AP*GP*CP*GP*CP*GP*CP*AP*GP*CP*CP*CP*TP*A)-3'), 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsmultiple drug resistance, ssdna binding, antibiotics, staphylococci, transcription-dna complex, transcription/dna
Biological sourceStaphylococcus epidermidis
Total number of polymer chains9
Total formula weight132947.17
Authors
Chang, Y.M.,Chen, C.K.-M.,Wang, A.H.-J. (deposition date: 2013-04-25, release date: 2014-03-19, Last modification date: 2023-09-20)
Primary citationChang, Y.M.,Ho, C.H.,Chen, C.K.,Maestre-Reyna, M.,Chang-Chien, M.W.,Wang, A.H.
TcaR-ssDNA complex crystal structure reveals new DNA binding mechanism of the MarR family proteins.
Nucleic Acids Res., 42:5314-5321, 2014
Cited by
PubMed Abstract: The teicoplanin-associated locus regulator (TcaR) regulates gene expression of proteins on the intercellular adhesion (ica) locus involved in staphylococci poly-N-acetylglucosamine biosynthesis. The absence of TcaR increases poly-N-acetylglucosamine production and promotes biofilm formation. Until recently, the mechanism of multiple antibiotic resistance regulator family protein members, such as TcaR, was restricted to binding double-stranded DNA. However, we recently found that TcaR strongly interacts with single-stranded DNA, which is a new role for this family of proteins. In this study, we report Staphylococcus epidermidis TcaR-single-stranded DNA complex structures. Our model suggests that TcaR and single-stranded DNA form a 61-symmetry polymer composed of TcaR dimers with single-stranded DNA that wraps outside the polymer and 12 nt per TcaR dimer. Single-stranded DNA binding to TcaR involves a large conformational change at the DNA binding lobe. Several point mutations involving the single-stranded DNA binding surface validate interactions between single-stranded DNA and TcaR. Our results extend the novel role of multiple antibiotic resistance regulator family proteins in staphylococci.
PubMed: 24531929
DOI: 10.1093/nar/gku128
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.6 Å)
Structure validation

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