X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster

Lee, Chi F.; Hauenstein, Arthur V.; Fleming, Jonathan K.; Gasper, William C.; Engelke, Valerie; Sankaran, Banumathi; Bernstein, Sanford I.; Huxford, Tom

doi:10.1016/j.str.2011.01.002

Title: X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster

Full Record
Other Related Research

Authors:: Lee, Chi F.; Hauenstein, Arthur V.; Fleming, Jonathan K.; Gasper, William C.; Engelke, Valerie; Sankaran, Banumathi; Bernstein, Sanford I.; Huxford, Tom

Publication Date:: Tue Mar 01 00:00:00 EST 2011

Sponsoring Org.:: USDOE

OSTI Identifier:: 1198407

Grant/Contract Number:: AC02-05CH11231

Resource Type:: Published Article

Journal Name:: Structure

Additional Journal Information:: Journal Name: Structure Journal Volume: 19 Journal Issue: 3; Journal ID: ISSN 0969-2126

Publisher:: Elsevier

Country of Publication:: United Kingdom

Language:: English

Citation Formats


                    Lee, Chi F., Hauenstein, Arthur V., Fleming, Jonathan K., Gasper, William C., Engelke, Valerie, Sankaran, Banumathi, Bernstein, Sanford I., and Huxford, Tom. X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster.  United Kingdom: N. p., 2011. 
Web.  doi:10.1016/j.str.2011.01.002.

Copy to clipboard


                    Lee, Chi F., Hauenstein, Arthur V., Fleming, Jonathan K., Gasper, William C., Engelke, Valerie, Sankaran, Banumathi, Bernstein, Sanford I., & Huxford, Tom. X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster.  United Kingdom.  https://doi.org/10.1016/j.str.2011.01.002

Copy to clipboard


                    Lee, Chi F., Hauenstein, Arthur V., Fleming, Jonathan K., Gasper, William C., Engelke, Valerie, Sankaran, Banumathi, Bernstein, Sanford I., and Huxford, Tom. Tue .  
"X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster".  United Kingdom.  https://doi.org/10.1016/j.str.2011.01.002.

Copy to clipboard


                    
@article{osti_1198407,

  title        = {X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster},

  author       = {Lee, Chi F. and Hauenstein, Arthur V. and Fleming, Jonathan K. and Gasper, William C. and Engelke, Valerie and Sankaran, Banumathi and Bernstein, Sanford I. and Huxford, Tom},

  abstractNote = {},

  doi          = {10.1016/j.str.2011.01.002},

  journal      = {Structure},

  number       = 3,

  volume       = 19,

  place        = {United Kingdom},

  year         = {Tue Mar 01 00:00:00 EST 2011},

  month        = {Tue Mar 01 00:00:00 EST 2011}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1016/j.str.2011.01.002

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 25 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

UNC-45/CRO1/She4p (UCS) Protein Forms Elongated Dimer and Joins Two Myosin Heads Near Their Actin Binding Region

Journal Article Shi, H ; Blobel, G - Proceedings of the National Academy of Sciences of the United States of America

UNC-45/CRO1/She4p (UCS) proteins have variously been proposed to affect the folding, stability, and ATPase activity of myosins. They are the only proteins known to interact directly with the motor domain. To gain more insight into UCS function, we determined the atomic structure of the yeast UCS protein, She4p, at 2.9 {angstrom} resolution. We found that 16 helical repeats are organized into an L-shaped superhelix with an amphipathic N-terminal helix dangling off the short arm of the L-shaped molecule. In the crystal, She4p forms a 193-{angstrom}-long, zigzag-shaped dimer through three distinct and evolutionary conserved interfaces. We have identified She4p's C-terminal regionmore »« less
Purification, isolation, crystallization, and preliminary X-ray diffraction study of the BTB domain of the centrosomal protein 190 from Drosophila melanogaster

Journal Article Boyko, K. M., E-mail: kmb@inbi.ras.ru ; Nikolaeva, A. Yu. ; Kachalova, G. S. ; ... - Crystallography Reports

The spatial organization of the genome is controlled by a special class of architectural proteins, including proteins containing BTB domains that are able to dimerize or multimerize. The centrosomal protein 190 is one of such architectural proteins. The purification, crystallization, and preliminary X-ray diffraction study of the BTB domain of the centrosomal protein 190 are reported. The crystallization conditions were found by the vapor-diffusion technique. The crystals diffracted to 1.5 Å resolution and belonged to sp. gr. P322{sub 1}. The structure was solved by the molecular replacement method. The structure refinement is currently underway.
https://doi.org/10.1134/S1063774517060050
Drosophila UNC-45 prevents heat-induced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase

Journal Article Melkani, Girish C. ; Lee, Chi F. ; Cammarato, Anthony ; ... - Biochemical and Biophysical Research Communications

UNC-45 belongs to the UCS (UNC-45, CRO1, She4p) domain protein family, whose members interact with various classes of myosin. Here we provide structural and biochemical evidence that Escherichia coli-expressed Drosophila UNC-45 (DUNC-45) maintains the integrity of several substrates during heat-induced stress in vitro. DUNC-45 displays chaperone function in suppressing aggregation of the muscle myosin heavy meromyosin fragment, the myosin S-1 motor domain, {alpha}-lactalbumin and citrate synthase. Biochemical evidence is supported by electron microscopy, which reveals the first structural evidence that DUNC-45 prevents inter- or intra-molecular aggregates of skeletal muscle heavy meromyosin caused by elevated temperatures. We also demonstrate for themore »« less
https://doi.org/10.1016/J.BBRC.2010.04.090
Preliminary small-angle X-ray scattering and X-ray diffraction studies of the BTB domain of lola protein from Drosophila melanogaster

Journal Article Boyko, K. M., E-mail: kmb@inbi.ras.ru ; Nikolaeva, A. Yu. ; Kachalova, G. S. ; ... - Crystallography Reports

The Drosophila genome has several dozens of transcription factors (TTK group) containing ВТВ domains assembled into octamers. The LOLA protein belongs to this family. The purification, crystallization, and preliminary X-ray diffraction and small-angle X-ray scattering (SAXS) studies of the BTB domain of this protein are reported. The crystallization conditions were found by the vapor-diffusion technique. A very low diffraction resolution (8.7 Å resolution) of the crystals was insufficient for the determination of the threedimensional structure of the BTB domain. The SAXS study demonstrated that the BTB domain of the LOLA protein exists as an octamer in solution.
https://doi.org/10.1134/S1063774517060062
Crystal structure of the Rasputin NTF2-like domain from Drosophila melanogaster

Journal Article Vognsen, Tina ; Kristensen, Ole - Biochemical and Biophysical Research Communications

Highlights: Black-Right-Pointing-Pointer The crystal structure of the NTF2-like domain of Rasputin protein is presented. Black-Right-Pointing-Pointer Differences to known ligand binding sites of nuclear transport factor 2 are discussed. Black-Right-Pointing-Pointer A new ligand binding site for the Rasputin and G3BP proteins is proposed. -- Abstract: The crystal structure of the NTF2-like domain of the Drosophila homolog of Ras GTPase SH3 Binding Protein (G3BP), Rasputin, was determined at 2.7 A resolution. The overall structure is highly similar to nuclear transport factor 2: It is a homodimer comprised of a {beta}-sheet and three {alpha}-helices forming a cone-like shape. However, known binding sites formore »« less
https://doi.org/10.1016/J.BBRC.2012.02.140

Similar Records