5A4N

Crystal structure of BPSL1147, a PC4 homolog from Burkholderia pseudomallei K96243 (tetragonal crystal form)

Summary for 5A4N

• Entry DOI: 10.2210/pdb5a4n/pdb
• Related: 5A4O
• Descriptor: BPSL1147, CHLORIDE ION (3 entities in total)
• Functional Keywords: dna-binding protein, transcription, dna replication, recombination and repair, dna binding protein
• Biological source: BURKHOLDERIA PSEUDOMALLEI
• Total number of polymer chains: 2
• Total formula weight: 17253.41

Authors

Werten, S.,Bayer, N.,Hinrichs, W. (deposition date: 2015-06-11, release date: 2016-04-06, Last modification date: 2024-01-10)

Primary citation

Werten, S.,Kohler, C.,Bayer, N.,Steinmetz, I.,Hinrichs, W.
Structural Analysis and Knock-Out of a Burkholderia Pseudomallei Homolog of the Eukaryotic Transcription Coactivator Pc4.
Gene, 557:140-, 2016

PubMed Abstract: Homologs of the eukaryotic transcription coactivator PC4, which also functions in DNA repair and oxidative stress, were recently identified in prokaryotes. Crystallographic analysis of BPSL1147, a putative homolog from the pathogen Burkholderia pseudomallei K96243, reveals a highly conserved core structure and suggests a nucleic acid binding mode similar to that of PC4. Knock-out and complementation experiments do not reveal distinguishing phenotypes under normal growth conditions or in the presence of H2O2, arguing against a critical role in repair or the oxidative stress response of Burkholderia. These results may reflect redundancy or point at a bacteriophage origin of Burkholderia PC4 homologs.

PubMed: 26625975
DOI: 10.1016/J.GENE.2015.11.037

Experimental method

X-RAY DIFFRACTION (1.96 Å)