This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4i2z

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 12:50, 25 December 2014

Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide

Structural highlights

4i2z is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	4i2w
Gene:	unc-45, CELE_F30H5.1, F30H5.1 (Caenorhabditis elegans)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[HSP90_CAEEL] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required to stabilize the daf-11/transmembrane guanylyl cyclases or another signal transduction component that regulates cGMP levels. Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation.^[1] ^[2]

Publication Abstract from PubMed

The UCS (UNC-45/CRO1/She4) chaperones play an evolutionarily conserved role in promoting myosin-dependent processes, including cytokinesis, endocytosis, RNA transport, and muscle development. To investigate the protein machinery orchestrating myosin folding and assembly, we performed a comprehensive analysis of Caenorhabditis elegans UNC-45. Our structural and biochemical data demonstrate that UNC-45 forms linear protein chains that offer multiple binding sites for cooperating chaperones and client proteins. Accordingly, Hsp70 and Hsp90, which bind to the TPR domain of UNC-45, could act in concert and with defined periodicity on captured myosin molecules. In vivo analyses reveal the elongated canyon of the UCS domain as a myosin-binding site and show that multimeric UNC-45 chains support organization of sarcomeric repeats. In fact, expression of transgenes blocking UNC-45 chain formation induces dominant-negative defects in the sarcomere structure and function of wild-type worms. Together, these findings uncover a filament assembly factor that directly couples myosin folding with myofilament formation.

The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans.,Gazda L, Pokrzywa W, Hellerschmied D, Lowe T, Forne I, Mueller-Planitz F, Hoppe T, Clausen T Cell. 2013 Jan 17;152(1-2):183-95. doi: 10.1016/j.cell.2012.12.025. PMID:23332754^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Birnby DA, Link EM, Vowels JJ, Tian H, Colacurcio PL, Thomas JH. A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegans. Genetics. 2000 May;155(1):85-104. PMID:10790386
↑ Inoue T, Hirata K, Kuwana Y, Fujita M, Miwa J, Roy R, Yamaguchi Y. Cell cycle control by daf-21/Hsp90 at the first meiotic prophase/metaphase boundary during oogenesis in Caenorhabditis elegans. Dev Growth Differ. 2006 Jan;48(1):25-32. PMID:16466390 doi:http://dx.doi.org/DGD
↑ Gazda L, Pokrzywa W, Hellerschmied D, Lowe T, Forne I, Mueller-Planitz F, Hoppe T, Clausen T. The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans. Cell. 2013 Jan 17;152(1-2):183-95. doi: 10.1016/j.cell.2012.12.025. PMID:23332754 doi:http://dx.doi.org/10.1016/j.cell.2012.12.025

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4i2z"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i2z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i2z RCSB], [http://www.ebi.ac.uk/pdbsum/4i2z PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/HSP90_CAEEL HSP90_CAEEL]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required to stabilize the daf-11/transmembrane guanylyl cyclases or another signal transduction component that regulates cGMP levels. Participates in the control of cell cycle progression at the prophase/metaphase transition in oocyte development by ensuring the activity of wee-1.3 kinase, which negatively regulates cdk-1 through its phosphorylation.<ref>PMID:10790386</ref> <ref>PMID:16466390</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4i2z

From Proteopedia

Revision as of 12:50, 25 December 2014

Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90 peptide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox