PDBsum entry 1quu

Contractile protein

PDB id: 1quu

Contents

Protein chain

248 a.a. *

Waters ×151

* Residue conservation analysis

PDB id:

1quu

Name:

Contractile protein

Title:

Crystal structure of two central spectrin-like repeats from alpha- actinin

Structure:

Human skeletal muscle alpha-actinin 2. Chain: a. Fragment: spectrin-like repeats 2 and 3 - amino acids 391 to 637. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Tissue: skeletal muscle. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

2.50Å R-factor: 0.229 R-free: 0.311

Authors:

K.Djinovic-Carugo,P.Young,M.Gautel,M.Saraste

Key ref:

K.Djinović-Carugo et al. (1999). Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell, 98, 537-546. PubMed id: 10481917 DOI: 10.1016/S0092-8674(00)81981-9

Date:

03-Jul-99 Release date: 20-Aug-99

Protein chain

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

Seq: 894 a.a.

Struc: 248 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/S0092-8674(00)81981-9

Cell 98:537-546 (1999)

PubMed id: 10481917

Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments.

K.Djinović-Carugo, P.Young, M.Gautel, M.Saraste.

ABSTRACT

We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments.

Selected figure(s)

Figure 3.
Figure 3. The Connecting LinkerClose-up of interactions between R2, R3, and the linker. The protein backbone is shown as a ribbon, and amino acid residues are drawn in a ball-and-stick representation. R2 is colored blue, R3 is green, and the linker is red.

Figure 6.
Figure 6. Model of the α-Actinin Rod(A) Sequence alignment of the α-actinin repeats used in modeling of repeats R1 and R4. Residue numbers for the full-length molecule and those of the construct used for the crystal structure are indicated at the edges and above the alignment, respectively. The α helices seen in the crystal structure are depicted as bars (blue for R2 and green for R3). The C termini of R1 and R3 and the N termini of R2 and R4, respectively, overlap due to the modeling procedure of R1 and R4. The overlapping residues shown in italic were used to assemble the model of the rod. The figure was generated with ALSCRIPT ([1]).(B) Ribbon diagram of α-actinin rod viewed in two orientations related by a 65 degree rotation around the long molecular axis through the central 2-fold axis. R1 is colored violet, R2 is blue, R3 is green, and R4 is yellow.(C) Electrostatic surface potential of one R1–R4 subunit generated with GRASP ([38]). Positively charged surface is colored blue and negatively charged red. The second subunit is white in a wormlike representation. Surfaces corresponding to R1 and R4 are marked.

The above figures are reprinted by permission from Cell Press: Cell (1999, 98, 537-546) copyright 1999.

Figures were selected by an automated process.