PDBsum entry 4git

Hydrolase

PDB id: 4git

Contents

Protein chains

92 a.a.

Ligands

SO4 ×2

Waters ×4

PDB id:

4git

Name:

Hydrolase

Title:

Crystal structure of alpha sub-domain of lon protease from brevibacillus thermoruber

Structure:

Lon protease. Chain: a, b. Fragment: alpha sub-domain, unp residues 491-605. Engineered: yes

Source:

Brevibacillus thermoruber. Organism_taxid: 33942. Strain: wr-249. Gene: lon. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.88Å R-factor: 0.206 R-free: 0.248

Authors:

Y.D.Chen,Y.Y.Chang,C.H.Hsu

Key ref:

A.Y.Lee et al. (2014). Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease. Acta Crystallogr D Biol Crystallogr, 70, 218-230. PubMed id: 24531457 DOI: 10.1107/S139900471302631X

Date:

09-Aug-12 Release date: 11-Sep-13

Protein chains

Q84FG5  (Q84FG5_9BACL) -  Lon protease from Brevibacillus thermoruber

Seq: 779 a.a.

Struc: 92 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.21.53 - endopeptidase La.
• Reaction: Hydrolysis of large proteins such as globin, casein and denaturated serum albumin, in presence of ATP.

DOI no: 10.1107/S139900471302631X

Acta Crystallogr D Biol Crystallogr 70:218-230 (2014)

PubMed id: 24531457

Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease.

A.Y.Lee, Y.D.Chen, Y.Y.Chang, Y.C.Lin, C.F.Chang, S.J.Huang, S.H.Wu, C.H.Hsu.

ABSTRACT

Lon belongs to a unique group of AAA(+) proteases that bind DNA. However, the DNA-mediated regulation of Lon remains elusive. Here, the crystal structure of the α subdomain of the Lon protease from Brevibacillus thermoruber (Bt-Lon) is presented, together with biochemical data, and the DNA-binding mode is delineated, showing that Arg518, Arg557 and Arg566 play a crucial role in DNA binding. Electrostatic interactions contributed by arginine residues in the AAA(+) module are suggested to be important to DNA binding and allosteric regulation of enzymatic activities. Intriguingly, Arg557, which directly binds DNA in the α subdomain, has a dual role in the negative regulation of ATPase stimulation by DNA and in the domain-domain communication in allosteric regulation of Bt-Lon by substrate. In conclusion, structural and biochemical evidence is provided to show that electrostatic interaction in the AAA(+) module is important for DNA binding by Lon and allosteric regulation of its enzymatic activities by DNA and substrate.