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TitleStructural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation.
Journal, issue, pagesNat Commun, Vol. 8, Issue 1, Page 1350, Year 2017
Publish dateNov 7, 2017
AuthorsAdam W Avery / Michael E Fealey / Fengbin Wang / Albina Orlova / Andrew R Thompson / David D Thomas / Thomas S Hays / Edward H Egelman /
PubMed AbstractSpinocerebellar ataxia type 5 (SCA5) is a neurodegenerative disease caused by mutations in the cytoskeletal protein β-III-spectrin. Previously, a SCA5 mutation resulting in a leucine-to-proline ...Spinocerebellar ataxia type 5 (SCA5) is a neurodegenerative disease caused by mutations in the cytoskeletal protein β-III-spectrin. Previously, a SCA5 mutation resulting in a leucine-to-proline substitution (L253P) in the actin-binding domain (ABD) was shown to cause a 1000-fold increase in actin-binding affinity. However, the structural basis for this increase is unknown. Here, we report a 6.9 Å cryo-EM structure of F-actin complexed with the L253P ABD. This structure, along with co-sedimentation and pulsed-EPR measurements, demonstrates that high-affinity binding caused by the CH2-localized mutation is due to opening of the two CH domains. This enables CH1 to bind actin aided by an unstructured N-terminal region that becomes α-helical upon binding. This helix is required for association with actin as truncation eliminates binding. Collectively, these results shed light on the mechanism by which β-III-spectrin, and likely similar actin-binding proteins, interact with actin, and how this mechanism can be perturbed to cause disease.
External linksNat Commun / PubMed:29116080 / PubMed Central
MethodsEM (helical sym.)
Resolution7.0 Å
Structure data

8886

6anu

EMDB-8886, PDB-6anu:
Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain
Method: EM (helical sym.) / Resolution: 7.0 Å

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / actin binding protein / filament

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