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2Q1N

Actin Dimer Cross-linked Between Residues 41 and 374

Summary for 2Q1N
Entry DOI10.2210/pdb2q1n/pdb
Related2A5X 2Q31 2Q36
DescriptorActin, alpha skeletal muscle, CALCIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
Functional Keywordscross-linked dimer, structural protein
Biological sourceOryctolagus cuniculus (rabbit)
Cellular locationCytoplasm, cytoskeleton: P68135
Total number of polymer chains2
Total formula weight85741.03
Authors
Sawaya, M.R.,Pashkov, I.,Kudryashov, D.S.,Adisetiyo, H.,Reisler, E.,Yeates, T.O. (deposition date: 2007-05-25, release date: 2007-06-05, Last modification date: 2023-08-30)
Primary citationSawaya, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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数据于2024-12-18公开中

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