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Complex of MlcC bound to the tandem IQ motif of MyoCComplex of MlcC bound to the tandem IQ motif of MyoC
Structural highlights
FunctionPublication Abstract from PubMedMyosin light chains are key regulators of class 1 myosins and typically comprise two domains, with calmodulin being the archetypal example. They bind IQ motifs within the myosin neck region and amplify conformational changes in motor domain. A single lobe light chain, myosin light chain C (MlcC), was recently identified and shown to specifically bind to two sequentially divergent IQ motifs of the Dictyostelium myosin-1C. Towards providing a molecular basis of this interaction, the structures of apo-MlcC and a 2:1 MlcC:myosin-1C neck complex were determined. The two non-functional EF-hand motifs of MlcC pack together to form a globular four-helix bundle that opens up to expose a central hydrophobic groove, which interacts the N-terminal portion of the divergent IQ1 and IQ2 motifs. N- and C-terminal regions of MlcC make critical contacts that contribute to its specific interactions with the myosin-1C divergent IQ motifs; contacts that deviate from the traditional mode of calmodulin-IQ recognition. Structure of the single-lobe myosin light chain C in complex with the light chain-binding domains of myosin-1C provides insights into divergent IQ-motif recognition.,Langelaan DN, Liburd J, Yang Y, Miller E, Chitayat S, Crawley SW, Cote GP, Smith SP J Biol Chem. 2016 Jul 27. pii: jbc.M116.746313. PMID:27466369[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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