2Q31

Actin Dimer Cross-linked Between Residues 41 and 374 and proteolytically cleaved by subtilisin between residues 47 and 48.

Summary for 2Q31

• Entry DOI: 10.2210/pdb2q31/pdb
• Related: 2A5X 2Q1N 2Q36
• Descriptor: Actin, alpha skeletal muscle, CALCIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: cross-linked dimer, proteolytically cleaved, structural protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 2
• Total formula weight: 85662.84

Authors

Sawaya, M.R.,Pashkov, I.,Kudryashov, D.S.,Reisler, E.,Yeates, T.O. (deposition date: 2007-05-29, release date: 2007-06-05, Last modification date: 2023-08-30)

Primary citation

Sawaya, M.R.,Kudryashov, D.S.,Pashkov, I.,Adisetiyo, H.,Reisler, E.,Yeates, T.O.
Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.
Acta Crystallogr.,Sect.D, 64:454-465, 2008

PubMed Abstract: The structure of actin in its monomeric form is known at high resolution, while the structure of filamentous F-actin is only understood at considerably lower resolution. Knowing precisely how the monomers of actin fit together would lead to a deeper understanding of the dynamic behavior of the actin filament. Here, a series of crystal structures of actin dimers are reported which were prepared by cross-linking in either the longitudinal or the lateral direction in the filament state. Laterally cross-linked dimers, comprised of monomers belonging to different protofilaments, are found to adopt configurations in crystals that are not related to the native structure of filamentous actin. In contrast, multiple structures of longitudinal dimers consistently reveal the same interface between monomers within a single protofilament. The reappearance of the same longitudinal interface in multiple crystal structures adds weight to arguments that the interface visualized is similar to that in actin filaments. Highly conserved atomic interactions involving residues 199-205 and 287-291 are highlighted.

PubMed: 18391412
DOI: 10.1107/S0907444908003351

Experimental method

X-RAY DIFFRACTION (2.7 Å)