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6rzb

From Proteopedia

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Current revision

Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain bound to microtubules

6rzb, resolution 5.00Å

Structural highlights

6rzb is a 3 chain structure with sequence from Mus musculus and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 5Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TBA1B_PIG Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Publication Abstract from PubMed

Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule.

Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.,Lacey SE, He S, Scheres SH, Carter AP Elife. 2019 Jul 2;8. pii: 47145. doi: 10.7554/eLife.47145. PMID:31264960^[1]

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

References

↑ Lacey SE, He S, Scheres SH, Carter AP. Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule. Elife. 2019 Jul 2;8. pii: 47145. doi: 10.7554/eLife.47145. PMID:31264960 doi:http://dx.doi.org/10.7554/eLife.47145

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6rzb"

@@ Line 3: / Line 3: @@
 <SX load='6rzb' size='340' side='right' viewer='molstar' caption='[[6rzb]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6rzb]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RZB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RZB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6rzb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RZB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RZB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dync1h1, Dnchc1, mKIAA0325 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rzb OCA], [http://pdbe.org/6rzb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rzb RCSB], [http://www.ebi.ac.uk/pdbsum/6rzb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rzb 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=6rzb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rzb OCA], [https://pdbe.org/6rzb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rzb RCSB], [https://www.ebi.ac.uk/pdbsum/6rzb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rzb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [[http://www.uniprot.org/uniprot/TBB_PIG TBB_PIG]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
+[https://www.uniprot.org/uniprot/TBA1B_PIG TBA1B_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 ==See Also==
+*[[Dynein 3D structures|Dynein 3D structures]]
 *[[Tubulin 3D Structures|Tubulin 3D Structures]]
 == References ==
@@ Line 27: / Line 28: @@
 </SX>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
 [[Category: Sus scrofa]]
-[[Category: Carter, A P]]
+[[Category: Carter AP]]
-[[Category: He, S]]
+[[Category: He S]]
-[[Category: Lacey, S E]]
+[[Category: Lacey SE]]
-[[Category: Scheres, S H.W]]
+[[Category: Scheres SHW]]
-[[Category: Complex]]
-[[Category: Filament]]
-[[Category: Motor protein]]

6rzb

From Proteopedia

Current revision

Cryo-EM structure of mouse cytoplasmic dynein-1 microtubule binding domain bound to microtubules

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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