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TitleCryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments.
Journal, issue, pagesNat Struct Mol Biol, Vol. 21, Issue 12, Page 1075-1081, Year 2014
Publish dateNov 2, 2014
AuthorsPeng Ge / Zeynep A Oztug Durer / Dmitri Kudryashov / Z Hong Zhou / Emil Reisler /
PubMed AbstractEssential 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- ...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-Pi mimic)-bound actin filaments in complex with the β-propeller domain of yeast coronin 1 (crn1), at 8.6-Å 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.
External linksNat Struct Mol Biol / PubMed:25362487 / PubMed Central
MethodsEM (helical sym.)
Resolution8.6 Å
Structure data

EMDB-6100:
CryoEM reveals different coronin binding modes for ADP- and ADP-BeFx- actin filaments
Method: EM (helical sym.) / Resolution: 8.6 Å

EMDB-6101:
CryoEM reveals different coronin binding modes for ADP- and ADP-BeFx- actin filaments
Method: EM (helical sym.) / Resolution: 8.6 Å

Source
  • Oryctolagus cuniculus (rabbit)
  • Saccharomyces cerevisiae (brewer's yeast)

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