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Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features.

ABSTRACT: A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. This complex serves as a model for the lever arm region of many classes of unconventional myosins, as well as other IQ motif-containing proteins such as neuromodulin and IQGAPs.

SUBMITTER: Houdusse A

PROVIDER: S-EPMC1687203 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature

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Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features.

Houdusse Anne A Gaucher Jean-François JF Krementsova Elena E Mui Suet S Trybus Kathleen M KM Cohen Carolyn C

Proceedings of the National Academy of Sciences of the United States of America 20061206 51

A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structur ...[more]

PMID: 17151196

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