4i2z

From Proteopedia

(Difference between revisions)

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?)

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