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4w8f

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Revision as of 15:50, 25 December 2014

Crystal structure of the dynein motor domain in the AMPPNP-bound state

Structural highlights

4w8f is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[DYHC_YEAST] Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.^[1]

Publication Abstract from PubMed

Dyneins power microtubule motility using ring-shaped, AAA-containing motor domains. Here, we report X-ray and electron microscopy (EM) structures of yeast dynein bound to different ATP analogs, which collectively provide insight into the roles of dynein's two major ATPase sites, AAA1 and AAA3, in the conformational change mechanism. ATP binding to AAA1 triggers a cascade of conformational changes that propagate to all six AAA domains and cause a large movement of the "linker," dynein's mechanical element. In contrast to the role of AAA1 in driving motility, nucleotide transitions in AAA3 gate the transmission of conformational changes between AAA1 and the linker, suggesting that AAA3 acts as a regulatory switch. Further structural and mutational studies also uncover a role for the linker in regulating the catalytic cycle of AAA1. Together, these results reveal how dynein's two major ATP-binding sites initiate and modulate conformational changes in the motor domain during motility.

Allosteric communication in the Dynein motor domain.,Bhabha G, Cheng HC, Zhang N, Moeller A, Liao M, Speir JA, Cheng Y, Vale RD Cell. 2014 Nov 6;159(4):857-68. doi: 10.1016/j.cell.2014.10.018. PMID:25417161^[2]

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

References

↑ Lee WL, Kaiser MA, Cooper JA. The offloading model for dynein function: differential function of motor subunits. J Cell Biol. 2005 Jan 17;168(2):201-7. Epub 2005 Jan 10. PMID:15642746 doi:http://dx.doi.org/10.1083/jcb.200407036
↑ Bhabha G, Cheng HC, Zhang N, Moeller A, Liao M, Speir JA, Cheng Y, Vale RD. Allosteric communication in the Dynein motor domain. Cell. 2014 Nov 6;159(4):857-68. doi: 10.1016/j.cell.2014.10.018. PMID:25417161 doi:http://dx.doi.org/10.1016/j.cell.2014.10.018

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/4w8f"

@@ Line 7: / Line 7: @@
 <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=4w8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w8f RCSB], [http://www.ebi.ac.uk/pdbsum/4w8f PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/DYHC_YEAST DYHC_YEAST]] Cytoplasmic dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle.<ref>PMID:15642746</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4w8f

From Proteopedia

Revision as of 15:50, 25 December 2014

Crystal structure of the dynein motor domain in the AMPPNP-bound state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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