2IX7

Structure of apo-calmodulin bound to unconventional myosin V

Summary for 2IX7

• Entry DOI: 10.2210/pdb2ix7/pdb
• Descriptor: CALMODULIN, MYOSIN-5A, SULFATE ION, ... (5 entities in total)
• Functional Keywords: contractile protein/metal binding, actin-binding, ubl conjugation, ca2+ regulation, myosin, calcium, iq motif, calmodulin, acetylation, nucleotide- binding, contractile protein, complex, phosphorylation, calmodulin-binding, metal binding, methylation, coiled coil, atp-binding, motor protein, contractile protein-metal binding complex
• Biological source: MUS MUSCULUS (HOUSE MOUSE); More
• Total number of polymer chains: 3
• Total formula weight: 40424.86

Authors

Houdusse, A.,Gaucher, J.F.,Mui, S.,Krementsova, E.,Trybus, K.M.,Cohen, C. (deposition date: 2006-07-07, release date: 2006-12-13, Last modification date: 2024-10-23)

Primary citation

Houdusse, A.,Gaucher, J.F.,Krementsova, E.,Mui, S.,Trybus, K.M.,Cohen, C.
Crystal Structure of Apo-Calmodulin Bound to the First Two Iq Motifs of Myosin V Reveals Essential Recognition Features.
Proc.Natl.Acad.Sci.USA, 103:19326-, 2006

PubMed 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.

PubMed: 17151196
DOI: 10.1073/PNAS.0609436103

Experimental method

X-RAY DIFFRACTION (2.5 Å)