X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster
| Autor: | Banumathi Sankaran, Sanford I. Bernstein, Valerie Engelke, Tom Huxford, Chi F. Lee, Jonathan K. Fleming, Arthur V. Hauenstein, William C. Gasper |
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| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Molecular Sequence Data Sequence alignment macromolecular substances Plasma protein binding Myosins Crystallography X-Ray Article Protein Structure Secondary Protein structure Structural Biology Myosin Scattering Small Angle Escherichia coli Animals Drosophila Proteins Amino Acid Sequence Caenorhabditis elegans Pliability Peptide sequence Molecular Biology Armadillo Domain Proteins biology biology.organism_classification Recombinant Proteins Protein Structure Tertiary Crystallography Drosophila melanogaster Armadillo repeats Chaperone (protein) Mutation biology.protein Biophysics Sequence Alignment Molecular Chaperones |
| Zdroj: | Structure. 19(3):397-408 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2011.01.002 |
| Popis: | UCS proteins, such as UNC-45, influence muscle contraction and other myosin-dependent motile processes. We report the first x-ray crystal structure of a UCS domain-containing protein, the UNC-45 myosin chaperone from Drosophila melanogaster (DmUNC-45). The structure reveals that the Central and UCS domains form a contiguous arrangement of seventeen consecutive helical layers that arrange themselves into five discrete armadillo repeat subdomains. Small-angle x-ray scattering data suggest that free DmUNC-45 adopts an elongated conformation and exhibits flexibility in solution. Protease sensitivity maps to a conserved loop that contacts the most carboxy-terminal UNC-45 armadillo repeat sub-domain. Amino acid conservation across diverse UCS proteins maps to one face of this carboxy-terminal sub-domain and the majority of mutations that affect myosin-dependent cellular activities lie within or around this region. Our crystallographic, biophysical, and biochemical analyses suggest that DmUNC-45 function is afforded by its flexibility and by structural integrity of its UCS domain. |
| Databáze: | OpenAIRE |
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