2BKI

Myosin VI nucleotide-free (MDinsert2-IQ) crystal structure

Summary for 2BKI

• Entry DOI: 10.2210/pdb2bki/pdb
• Related: 1AHR 2BKH
• Descriptor: UNCONVENTIONAL MYOSIN, CALMODULIN, SULFATE ION, ... (5 entities in total)
• Functional Keywords: motor protein-metal-binding protein complex, complex (motor protein-calmodulin), myosin vi, reverse myosin, calmodulin, iq motif, non- conventional myosin, nucleotide-free conformation, muscle protein, motor protein/metal-binding protein
• Biological source: SUS SCROFA (PIG); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein : Q29122
• Total number of polymer chains: 3
• Total formula weight: 132247.10

Authors

Menetrey, J.,Bahloul, A.,Yengo, C.,Wells, A.,Morris, C.,Sweeney, H.L.,Houdusse, A. (deposition date: 2005-02-16, release date: 2005-06-07, Last modification date: 2023-12-13)

Primary citation

Menetrey, J.,Bahloul, A.,Wells, A.,Yengo, C.,Morris, C.,Sweeney, H.L.,Houdusse, A.
The Structure of the Myosin Vi Motor Reveals the Mechanism of Directionality Reversal
Nature, 435:779-, 2005

PubMed Abstract: Here we solve a 2.4-A structure of a truncated version of the reverse-direction myosin motor, myosin VI, that contains the motor domain and binding sites for two calmodulin molecules. The structure reveals only minor differences in the motor domain from that in plus-end directed myosins, with the exception of two unique inserts. The first is near the nucleotide-binding pocket and alters the rates of nucleotide association and dissociation. The second unique insert forms an integral part of the myosin VI converter domain along with a calmodulin bound to a novel target motif within the insert. This serves to redirect the effective 'lever arm' of myosin VI, which includes a second calmodulin bound to an 'IQ motif', towards the pointed (minus) end of the actin filament. This repositioning largely accounts for the reverse directionality of this class of myosin motors. We propose a model incorporating a kinesin-like uncoupling/docking mechanism to provide a full explanation of the movements of myosin VI.

PubMed: 15944696
DOI: 10.1038/NATURE03592

Experimental method

X-RAY DIFFRACTION (2.9 Å)