5FBM
Crystal Structure of Histone Like Protein (HLP) from Streptococcus mutans Refined to 1.9 A Resolution
Summary for 5FBM
| Entry DOI | 10.2210/pdb5fbm/pdb |
| Descriptor | DNA-binding protein HU (2 entities in total) |
| Functional Keywords | histone-like protein, dna binding, dimerization, dna binding protein |
| Biological source | Streptococcus mutans serotype c (strain ATCC 700610 / UA159) |
| Total number of polymer chains | 2 |
| Total formula weight | 21658.84 |
| Authors | Lovell, S.,Battaile, K.P.,Mehzabeen, N.,O'Neil, P.,Biswas, I. (deposition date: 2015-12-14, release date: 2016-04-06, Last modification date: 2023-09-27) |
| Primary citation | O'Neil, P.,Lovell, S.,Mehzabeen, N.,Battaile, K.,Biswas, I. Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 angstrom resolution. Acta Crystallogr F Struct Biol Commun, 72:257-262, 2016 Cited by PubMed 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. PubMed: 27050257DOI: 10.1107/S2053230X1600217X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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