6JYI

Crystal structure of the PadR-like transcriptional regulator BC1756 from Bacillus cereus

Summary for 6JYI

• Entry DOI: 10.2210/pdb6jyi/pdb
• Descriptor: Transcriptional repressor PadR (2 entities in total)
• Functional Keywords: transcription factor, transcription
• Biological source: Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
• Total number of polymer chains: 2
• Total formula weight: 44394.33

Authors

Kim, T.H.,Park, S.C.,Lee, K.C.,Song, W.S.,Yoon, S.I. (deposition date: 2019-04-26, release date: 2019-06-26, Last modification date: 2024-10-30)

Primary citation

Kim, T.H.,Park, S.C.,Lee, K.C.,Song, W.S.,Yoon, S.I.
Structural and DNA-binding studies of the PadR-like transcriptional regulator BC1756 from Bacillus cereus.
Biochem.Biophys.Res.Commun., 515:607-613, 2019

PubMed Abstract: Transcription factors that belong to the PadR family play an essential role in the transcriptional regulation of diverse biological processes by recognizing their cognate palindromic DNA sequences. Bacillus cereus harbors a gene that encodes a PadR-like protein (bcPLP; BC1756). bcPLP has not been structurally characterized, and it remains unelucidated how bcPLP interacts with a specific DNA sequence to function as a transcription factor. To provide structural insights into DNA recognition by bcPLP, we performed a structural study and a DNA-binding analysis of bcPLP. The crystal structure of bcPLP was determined at 1.92 Å resolution. bcPLP consists of two domains, an N-terminal domain (NTD) and a C-terminal domain (CTD), and forms a homodimer mainly using the CTD. In the structure, bcPLP contains a highly positively charged elongated patch in the NTD that serves as a putative DNA-binding site. Indeed, an electrophoresis mobility shift assay and a fluorescence polarization assay showed that bcPLP specifically recognizes a palindromic DNA sequence upstream of the bcPLP-encoding region. Moreover, based on our mutagenesis and modeling studies, we demonstrate that bcPLP interacts with dsDNA primarily using the Y19, Y41, P64, and K66 residues in the NTD.

PubMed: 31178139
DOI: 10.1016/j.bbrc.2019.05.141

Experimental method

X-RAY DIFFRACTION (1.92 Å)