5owo

From Proteopedia

(Difference between revisions)

Current revision

Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution

Structural highlights

5owo is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.79Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

DYHC1_HUMAN Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures;Autosomal dominant non-syndromic intellectual disability;Autosomal dominant Charcot-Marie-Tooth disease type 2O. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

DYHC1_HUMAN Cytoplasmic dynein 1 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. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074).^[1]

Publication Abstract from PubMed

Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 A resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.

Cryo-EM shows how dynactin recruits two dyneins for faster movement.,Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470^[2]

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

References

↑ Chu X, Chen X, Wan Q, Zheng Z, Du Q. Nuclear Mitotic Apparatus (NuMA) Interacts with and Regulates Astrin at the Mitotic Spindle. J Biol Chem. 2016 Sep 16;291(38):20055-67. doi: 10.1074/jbc.M116.724831. Epub, 2016 Jul 26. PMID:27462074 doi:http://dx.doi.org/10.1074/jbc.M116.724831
↑ Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP. Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470 doi:http://dx.doi.org/10.1038/nature25462

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5owo"

@@ Line 1: / Line 1: @@
 ==Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution==
-<StructureSection load='5owo' size='340' side='right' caption='[[5owo]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
+<StructureSection load='5owo' size='340' side='right'caption='[[5owo]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5owo]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OWO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OWO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5owo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OWO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<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=5owo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5owo OCA], [http://pdbe.org/5owo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5owo RCSB], [http://www.ebi.ac.uk/pdbsum/5owo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5owo ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5owo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5owo OCA], [https://pdbe.org/5owo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5owo RCSB], [https://www.ebi.ac.uk/pdbsum/5owo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5owo ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN]] Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures;Autosomal dominant non-syndromic intellectual disability;Autosomal dominant Charcot-Marie-Tooth disease type 2O. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
+[https://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN] Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures;Autosomal dominant non-syndromic intellectual disability;Autosomal dominant Charcot-Marie-Tooth disease type 2O. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN]] Cytoplasmic dynein 1 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. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074).<ref>PMID:27462074</ref>
+[https://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN] Cytoplasmic dynein 1 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. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074).<ref>PMID:27462074</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 </div>
 <div class="pdbe-citations 5owo" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Dynein 3D structures|Dynein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Carter, A P]]
+[[Category: Homo sapiens]]
-[[Category: Elshenawy, M M]]
+[[Category: Large Structures]]
-[[Category: Lau, C K]]
+[[Category: Carter AP]]
-[[Category: Morales-Rios, E]]
+[[Category: Elshenawy MM]]
-[[Category: Motz, C]]
+[[Category: Lau CK]]
-[[Category: Urnavicius, L]]
+[[Category: Morales-Rios E]]
-[[Category: Yildiz, A]]
+[[Category: Motz C]]
-[[Category: Dimerization domain]]
+[[Category: Urnavicius L]]
-[[Category: Dynein]]
+[[Category: Yildiz A]]
-[[Category: Heavy chain]]
-[[Category: Motor protein]]

5owo

From Proteopedia

Current revision

Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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