5DYM

Crystal structure of a PadR family transcription regulator from hypervirulent Clostridium difficile R20291 - CdPadR_0991 to 1.89 Angstrom resolution

Summary for 5DYM

• Entry DOI: 10.2210/pdb5dym/pdb
• Descriptor: PadR-family transcriptional regulator (2 entities in total)
• Functional Keywords: padr, whth dna binding domain, helix turn helix motifs, transcription regulator, padr-s2, dna binding protein
• Biological source: Peptoclostridium difficile (strain R20291)
• Total number of polymer chains: 1
• Total formula weight: 14112.26

Authors

Isom, C.E.,Karr, E.A.,Menon, S.K.,West, A.H.,Richter-Addo, G.B. (deposition date: 2015-09-24, release date: 2016-10-05, Last modification date: 2023-09-27)

Primary citation

Isom, C.E.,Menon, S.K.,Thomas, L.M.,West, A.H.,Richter-Addo, G.B.,Karr, E.A.
Crystal structure and DNA binding activity of a PadR family transcription regulator from hypervirulent Clostridium difficile R20291.
Bmc Microbiol., 16:231-231, 2016

PubMed Abstract: Clostridium difficile is a spore-forming obligate anaerobe that can remain viable for extended periods, even in the presence of antibiotics, which contributes to the persistence of this bacterium as a human pathogen during host-to-host transmission and in hospital environments. We examined the structure and function of a gene product with the locus tag CDR20291_0991 (cdPadR1) as part of our broader goal aimed at elucidating transcription regulatory mechanisms involved in virulence and antibiotic resistance of the recently emergent hypervirulent C. difficile strain R20291. cdPadR1 is genomically positioned near genes that are involved in stress response and virulence. In addition, it was previously reported that cdPadR1 and a homologue from the historical C. difficile strain 630 (CD630_1154) were differentially expressed when exposed to stressors, including antibiotics.

PubMed: 27716049
DOI: 10.1186/s12866-016-0850-0

Experimental method

X-RAY DIFFRACTION (1.894 Å)