Structural highlights
FunctionDBH_STRMU Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Seems also to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs and acting as a nidus for in situ immune complex formation. Publication Abstract from PubMedNucleoid-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 A 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. Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 A resolution.,O'Neil P, Lovell S, Mehzabeen N, Battaile K, Biswas I Acta Crystallogr F Struct Biol Commun. 2016 Apr;72(Pt 4):257-62. doi:, 10.1107/S2053230X1600217X. Epub 2016 Mar 16. PMID:27050257[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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