Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 21, Issue 12, Pages 1075-1081Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2907
Keywords
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Funding
- US National Institutes of Health (US NIH) [GM077190, GM071940, AI094386, F32HL119069, 1S1ORR23057]
- American Heart Association [13P0ST17340020]
- Ohio State University
- CNSI at UCLA
- NATIONAL CENTER FOR RESEARCH RESOURCES [S10RR023057] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [F32HL119069] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI094386] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM077190, R01GM071940] Funding Source: NIH RePORTER
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Essential cellular processes involving the actin cytoskeleton are regulated by auxiliary proteins that can sense the nucleotide state of actin. Here we report cryo-EM structures for ADP-bound and ADP-beryllium fluoride (ADP-BeFx, an ADP-P-i mimic)-bound actin filaments in complex with the beta-propeller domain of yeast coronin 1 (crn1), at 8.6-angstrom resolution. Our structures reveal the main differences in the interaction of coronin with the two nucleotide states of F-actin. We derived pseudoatomic models by fitting the atomic structures of actin and coronin into the EM envelopes and confirmed the identified interfaces on actin by chemical cross-linking, fluorescence spectroscopy and actin mutagenesis. The models offer a structural explanation for the nucleotide-dependent effects of coronin on cofilin-assisted remodeling of F-actin.
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