4BYF
Crystal structure of human Myosin 1c in complex with calmodulin in the pre-power stroke state
Summary for 4BYF
| Entry DOI | 10.2210/pdb4byf/pdb |
| Descriptor | UNCONVENTIONAL MYOSIN-IC, CALMODULIN, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, myo1c, glut4 exocytosis, atpase, motor protein |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Isoform 1: Cytoplasm. Isoform 2: Cytoplasm. Isoform 3: Nucleus, nucleoplasm: O00159 Cytoplasm, cytoskeleton, spindle: P62158 |
| Total number of polymer chains | 4 |
| Total formula weight | 202745.69 |
| Authors | Munnich, S.,Taft, M.H.,Pathan-Chhatbar, S.,Manstein, D.J. (deposition date: 2013-07-19, release date: 2014-03-26, Last modification date: 2023-12-20) |
| Primary citation | Munnich, S.,Taft, M.H.,Manstein, D.J. Crystal Structure of Human Myosin 1C-the Motor in Glut4 Exocytosis: Implications for Ca(2+) Regulation and 14-3-3 Binding. J.Mol.Biol., 426:2070-, 2014 Cited by PubMed Abstract: Myosin 1c (Myo1c) plays a key role in supporting motile events that underlie cell migration, vesicle trafficking, insulin-stimulated glucose uptake and hearing. Here, we present the crystal structure of the human Myo1c motor in complex with its light chain calmodulin. Our structure reveals tight interactions of the motor domain with calmodulin bound to the first IQ motif in the neck region. Several of the calmodulin residues contributing to this interaction are also involved in Ca(2+) binding. Contact residues in the motor domain are linked to the central β-sheet and the HO helix, suggesting a mechanism for communicating changes in Ca(2+) binding in the neck region to the actin and nucleotide binding regions of the motor domain. The structural context and the chemical environment of Myo1c mutations that are involved in sensorineural hearing loss in humans are described and their impact on motor function is discussed. We show that a construct consisting of the motor domain of Myo1c and the first IQ motif is sufficient to establish a tight interaction with 14-3-3β (KD=0.9 μM) and present the model of a double-headed Myo1c-14-3-3 complex. This complex has been implicated in the exocytosis of glucose transporter 4 storage vesicles during insulin-stimulated glucose uptake. PubMed: 24636949DOI: 10.1016/J.JMB.2014.03.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.74 Å) |
Structure validation
Download full validation report
