PDBsum entry 3k1j

Hydrolase

PDB id: 3k1j

Contents

Protein chains

566 a.a. *

Ligands

ADP ×2

PE8

PE4

Waters ×835

* Residue conservation analysis

PDB id:

3k1j

Name:

Hydrolase

Title:

Crystal structure of lon protease from thermococcus onnurineus na1

Structure:

Atp-dependent protease lon. Chain: a, b. Synonym: lon protease. Engineered: yes. Mutation: yes

Source:

Thermococcus onnurineus. Organism_taxid: 523850. Strain: na1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.206 R-free: 0.235

Authors:

S.S.Cha,Y.J.An

Key ref:

S.S.Cha et al. (2010). Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber. Embo J, 29, 3520-3530. PubMed id: 20834233

Date:

28-Sep-09 Release date: 22-Sep-10

Protein chains

B6YU74  (B6YU74_THEON) -  Archaeal Lon protease from Thermococcus onnurineus (strain NA1)

Seq: 635 a.a.

Struc: 566 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Embo J 29:3520-3530 (2010)

PubMed id: 20834233

Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.

S.S.Cha, Y.J.An, C.R.Lee, H.S.Lee, Y.G.Kim, S.J.Kim, K.K.Kwon, G.M.De Donatis, J.H.Lee, M.R.Maurizi, S.G.Kang.

ABSTRACT

Lon proteases are distributed in all kingdoms of life and are required for survival of cells under stress. Lon is a tandem fusion of an AAA+ molecular chaperone and a protease with a serine-lysine catalytic dyad. We report the 2.0-Å resolution crystal structure of Thermococcus onnurineus NA1 Lon (TonLon). The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the AAA+ domain combine with an insertion domain containing the membrane anchor to form an apical domain that serves as a gate governing substrate access to an internal unfolding and degradation chamber. Alternating AAA+ domains are in tight- and weak-binding nucleotide states with different domain orientations and intersubunit contacts, reflecting intramolecular dynamics during ATP-driven protein unfolding and translocation. The bowl-shaped proteolytic chamber is contiguous with the chaperone chamber allowing internalized proteins direct access to the proteolytic sites without further gating restrictions.