2Q31: Actin Dimer Cross-linked Between Residues 41 And 374 And Proteolytically Cleaved By Subtilisin Between Residues 47 And 48

Citation:
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.
PDB ID: 2Q31Download
MMDB ID: 46752
PDB Deposition Date: 2007/5/29
Updated in MMDB: 2008/12
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 2Q31: dimeric; determined by author
Molecular Components in 2Q31
Label Count Molecule
Proteins (2 molecules)
2
Actin, Alpha Skeletal Muscle
Molecule annotation
Chemicals (6 molecules)
1
2
2
2
3
2
* Click molecule labels to explore molecular sequence information.

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