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Acta Crystallogr F Struct Biol Commun. 2016 Apr;72(Pt 4):257-62. doi: 10.1107/S2053230X1600217X. Epub 2016 Mar 16.

Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution.

Author information

1
Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA.
2
Protein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Kansas City, KS 66047, USA.
3
IMCA-CAT, Hauptman-Woodward Medical Research Institute, APS, Argonne National Laboratory, Argonne, IL 60439, USA.

Abstract

Nucleoid-associated proteins (NAPs) in prokaryotes play an important architectural role in DNA bending, supercoiling and DNA compaction. In addition to architectural roles, some NAPs also play regulatory roles in DNA replication and repair, and act as global transcriptional regulators in many bacteria. Bacteria encode multiple NAPs and some of them are even essential for survival. Streptococcus mutans, a dental pathogen, encodes one such essential NAP called histone-like protein (HLP). Here, the three-dimensional structure of S. mutans HLP has been determined to 1.9 Å resolution. The HLP structure is a dimer and shares a high degree of similarity with other bacterial NAPs, including HU. Since HLPs are essential for the survival of pathogenic streptococci, this structure determination is potentially beneficial for future drug development against these pathogens.

KEYWORDS:

HLP; Streptococcus mutans; histone-like protein; nucleoid-associated protein

PMID:
27050257
PMCID:
PMC4822980
DOI:
10.1107/S2053230X1600217X
[Indexed for MEDLINE]
Free PMC Article

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