5IBW

Complex of MlcC bound to the tandem IQ motif of MyoC

Summary for 5IBW

• Entry DOI: 10.2210/pdb5ibw/pdb
• Descriptor: Calcium-binding EF-hand domain-containing protein, Myosin IC heavy chain, SODIUM ION, ... (4 entities in total)
• Functional Keywords: myosin iq motif complex, motor protein
• Biological source: Dictyostelium discoideum (Slime mold); More
• Total number of polymer chains: 3
• Total formula weight: 23323.12

Authors

Langelaan, D.N.,Smith, S.P. (deposition date: 2016-02-22, release date: 2016-08-03, Last modification date: 2023-09-27)

Primary citation

Langelaan, D.N.,Liburd, J.,Yang, Y.,Miller, E.,Chitayat, S.,Crawley, S.W.,Cote, G.P.,Smith, S.P.
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.
J.Biol.Chem., 291:19607-19617, 2016

PubMed Abstract: Myosin 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 the 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. To provide 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 with the N-terminal portion of the divergent IQ1 and IQ2 motifs. The N- and C-terminal regions of MlcC make critical contacts that contribute to its specific interactions with the myosin-1C divergent IQ motifs, which are contacts that deviate from the traditional mode of calmodulin-IQ recognition.

PubMed: 27466369
DOI: 10.1074/jbc.M116.746313

Experimental method

X-RAY DIFFRACTION (1.9 Å)