PDBsum entry 5aj2

Apoptosis

PDB id: 5aj2

Contents

Protein chains

263 a.a.*

225 a.a.*

416 a.a.*

* C-alpha coords only

PDB id:

5aj2

Name:

Apoptosis

Title:

Cryo electron tomography of the naip5-nlrc4 inflammasome

Structure:

Nlr family card domain-containing protein 4. Chain: a. Fragment: residues 1-355. Synonym: caspase recruitment domain-containing protein 12, ice protease-activating factor, ipaf. Engineered: yes. Nlr family card domain-containing protein 4. Chain: b. Fragment: residues 356-580.

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293e.

Authors:

C.A.Diebolder,E.F.Halff,A.J.Koster,E.G.Huizinga,R.I.Koning

Key ref:

C.A.Diebolder et al. (2015). Cryoelectron Tomography of the NAIP5/NLRC4 Inflammasome: Implications for NLR Activation. Structure, 23, 2349-2357. PubMed id: 26585513 DOI: 10.1016/j.str.2015.10.001

Date:

20-Feb-15 Release date: 11-Nov-15

Protein chain

Q3UP24  (NLRC4_MOUSE) -  NLR family CARD domain-containing protein 4 from Mus musculus

Seq: 1024 a.a.

Struc: 263 a.a.

Protein chain

Q3UP24  (NLRC4_MOUSE) -  NLR family CARD domain-containing protein 4 from Mus musculus

Seq: 1024 a.a.

Struc: 225 a.a.

Protein chain

Q3UP24  (NLRC4_MOUSE) -  NLR family CARD domain-containing protein 4 from Mus musculus

Seq: 1024 a.a.

Struc: 416 a.a.

reference

DOI no: 10.1016/j.str.2015.10.001

Structure 23:2349-2357 (2015)

PubMed id: 26585513

Cryoelectron Tomography of the NAIP5/NLRC4 Inflammasome: Implications for NLR Activation.

C.A.Diebolder, E.F.Halff, A.J.Koster, E.G.Huizinga, R.I.Koning.

ABSTRACT

Inflammasomes are high molecular weight protein complexes that play a crucial role in innate immunity by activating caspase-1. Inflammasome formation is initiated when molecules originating from invading microorganisms activate nucleotide-binding domain and leucine-rich repeat-containing receptors (NLRs) and induce NLR multimerization. Little is known about the conformational changes involved in NLR activation and the structural organization of NLR multimers. Here, we show by cryoelectron tomography that flagellin-induced NAIP5/NLRC4 multimers form right- and left-handed helical polymers with a diameter of 28 nm and a pitch of 6.5 nm. Subtomogram averaging produced an electron density map at 4 nm resolution, which was used for rigid body fitting of NLR subdomains derived from the crystal structure of dormant NLRC4. The resulting structural model of inflammasome-incorporated NLRC4 indicates that a prominent rotation of the LRR domain of NLRC4 is necessary for multimer formation, providing unprecedented insight into the conformational changes that accompany NLR activation.