PDBsum entry 5fbm

DNA binding protein

PDB id: 5fbm

Contents

Protein chains

83 a.a.

83 a.a.

Waters ×60

PDB id:

5fbm

Name:

DNA binding protein

Title:

Crystal structure of histone like protein (hlp) from streptococcus mutans refined to 1.9 a resolution

Structure:

DNA-binding protein hu. Chain: a, b. Engineered: yes

Source:

Streptococcus mutans serotypE C (strain atcc 700610 / ua159). Organism_taxid: 210007. Strain: atcc 700610 / ua159. Gene: hup, hlpa, smu_589. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.90Å R-factor: 0.179 R-free: 0.217

Authors:

S.Lovell,K.P.Battaile,N.Mehzabeen,P.O'Neil,I.Biswas

Key ref:

P.O'Neil et al. (2016). Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution. Acta Crystallogr F Struct Biol Commun, 72, 257-262. PubMed id: 27050257

Date:

14-Dec-15 Release date: 06-Apr-16

Protein chain

Q9XB21  (DBH_STRMU) -  DNA-binding protein HU from Streptococcus mutans serotype c (strain ATCC 700610 / UA159)

Seq: 91 a.a.

Struc: 83 a.a.

Protein chain

Q9XB21  (DBH_STRMU) -  DNA-binding protein HU from Streptococcus mutans serotype c (strain ATCC 700610 / UA159)

Seq: 91 a.a.

Struc: 83 a.a.

Acta Crystallogr F Struct Biol Commun 72:257-262 (2016)

PubMed id: 27050257

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

P.O'Neil, S.Lovell, N.Mehzabeen, K.Battaile, I.Biswas.

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.