3NOW

UNC-45 from Drosophila melanogaster

Summary for 3NOW

• Entry DOI: 10.2210/pdb3now/pdb
• Descriptor: UNC-45 protein, SD10334p (1 entity in total)
• Functional Keywords: armadillo repeat, hsp90, myosin, tetra-tricopeptide repeat, tpr, binding protein required for myosin function, protein binding
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 89813.52

Authors

Lee, C.F.,Hauenstein, A.V.,Fleming, J.K.,Gasper, W.C.,Engelke, V.,Banumathi, S.,Bernstein, S.I.,Huxford, T. (deposition date: 2010-06-25, release date: 2011-03-16, Last modification date: 2023-12-27)

Primary citation

Lee, C.F.,Hauenstein, A.V.,Fleming, J.K.,Gasper, W.C.,Engelke, V.,Sankaran, B.,Bernstein, S.I.,Huxford, T.
X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster.
Structure, 19:397-408, 2011

PubMed Abstract: 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 17 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 subdomain. Amino acid conservation across diverse UCS proteins maps to one face of this carboxy-terminal subdomain, 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.

PubMed: 21397190
DOI: 10.1016/j.str.2011.01.002

Experimental method

X-RAY DIFFRACTION (2.992 Å)