PDBsum entry 4d1e

Contractile protein

PDB id: 4d1e

Contents

Protein chain

859 a.a.

PDB id:

4d1e

Name:

Contractile protein

Title:

The crystal structure of human muscle alpha-actinin-2

Structure:

Alpha-actinin-2. Chain: a. Fragment: residues 19-894. Synonym: alpha-actinin skeletal muscle isoform 2, f-actin cross- linking protein. Engineered: yes. Mutation: yes. Other_details: delta 1-18 lysine methylation

Source:

Homo sapiens. Human. Organism_taxid: 9606. Tissue: muscle. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta plyss.

Resolution:

3.50Å R-factor: 0.207 R-free: 0.258

Authors:

N.Pinotsis,A.Salmazo,B.Sjoeblom,E.Gkougkoulia,K.Djinovic-Carugo

Key ref:

E.d.e. .A.Ribeiro et al. (2014). The structure and regulation of human muscle α-actinin. Cell, 159, 1447-1460. PubMed id: 25433700 DOI: 10.1016/j.cell.2014.10.056

Date:

01-May-14 Release date: 10-Dec-14

Protein chain

P35609  (ACTN2_HUMAN) -  Alpha-actinin-2 from Homo sapiens

Seq: 894 a.a.

Struc: 859 a.a.*

* PDB and UniProt seqs differ at 15 residue positions (black crosses)

DOI no: 10.1016/j.cell.2014.10.056

Cell 159:1447-1460 (2014)

PubMed id: 25433700

The structure and regulation of human muscle α-actinin.

E.d.e. .A.Ribeiro, N.Pinotsis, A.Ghisleni, A.Salmazo, P.V.Konarev, J.Kostan, B.Sjöblom, C.Schreiner, A.A.Polyansky, E.A.Gkougkoulia, M.R.Holt, F.L.Aachmann, B.Zagrović, E.Bordignon, K.F.Pirker, D.I.Svergun, M.Gautel, K.Djinović-Carugo.

ABSTRACT

The spectrin superfamily of proteins plays key roles in assembling the actin cytoskeleton in various cell types, crosslinks actin filaments, and acts as scaffolds for the assembly of large protein complexes involved in structural integrity and mechanosensation, as well as cell signaling. α-actinins in particular are the major actin crosslinkers in muscle Z-disks, focal adhesions, and actin stress fibers. We report a complete high-resolution structure of the 200 kDa α-actinin-2 dimer from striated muscle and explore its functional implications on the biochemical and cellular level. The structure provides insight into the phosphoinositide-based mechanism controlling its interaction with sarcomeric proteins such as titin, lays a foundation for studying the impact of pathogenic mutations at molecular resolution, and is likely to be broadly relevant for the regulation of spectrin-like proteins.