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.


3j6p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:28, 20 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 3: Line 3:
<SX load='3j6p' size='340' side='right' viewer='molstar' caption='[[3j6p]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
<SX load='3j6p' size='340' side='right' viewer='molstar' caption='[[3j6p]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3j6p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi] 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=3J6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J6P FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3j6p]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] 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=3J6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J6P FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 8.2&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB_G0276355, dhcA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6p OCA], [http://pdbe.org/3j6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j6p RCSB], [http://www.ebi.ac.uk/pdbsum/3j6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j6p 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=3j6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6p OCA], [https://pdbe.org/3j6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j6p RCSB], [https://www.ebi.ac.uk/pdbsum/3j6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j6p ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/DYHC_DICDI DYHC_DICDI]] 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. [[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. [[http://www.uniprot.org/uniprot/TBA1A_PIG TBA1A_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/DYHC_DICDI DYHC_DICDI] 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.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Dynein is a motor protein that moves on microtubules (MTs) using the energy of adenosine triphosphate (ATP) hydrolysis. To understand its motility mechanism, it is crucial to know how the signal of MT binding is transmitted to the ATPase domain to enhance ATP hydrolysis. However, the molecular basis of signal transmission at the dynein-MT interface remains unclear. Scanning mutagenesis of tubulin identified two residues in alpha-tubulin, R403 and E416, that are critical for ATPase activation and directional movement of dynein. Electron cryomicroscopy and biochemical analyses revealed that these residues form salt bridges with the residues in the dynein MT-binding domain (MTBD) that work in concert to induce registry change in the stalk coiled coil and activate the ATPase. The R403-E3390 salt bridge functions as a switch for this mechanism because of its reversed charge relative to other residues at the interface. This study unveils the structural basis for coupling between MT binding and ATPase activation and implicates the MTBD in the control of directional movement.
+
-
 
+
-
A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation.,Uchimura S, Fujii T, Takazaki H, Ayukawa R, Nishikawa Y, Minoura I, Hachikubo Y, Kurisu G, Sutoh K, Kon T, Namba K, Muto E J Cell Biol. 2015 Jan 19;208(2):211-22. doi: 10.1083/jcb.201407039. Epub 2015 Jan, 12. PMID:25583999<ref>PMID:25583999</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3j6p" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Dynein 3D structures|Dynein 3D structures]]
*[[Dynein 3D structures|Dynein 3D structures]]
-
*[[Tubulin|Tubulin]]
+
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</SX>
</SX>
-
[[Category: Dicdi]]
+
[[Category: Dictyostelium discoideum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
-
[[Category: Ayukawa, R]]
+
[[Category: Ayukawa R]]
-
[[Category: Fujii, T]]
+
[[Category: Fujii T]]
-
[[Category: Hachikubo, Y]]
+
[[Category: Hachikubo Y]]
-
[[Category: Kon, T]]
+
[[Category: Kon T]]
-
[[Category: Kurisu, G]]
+
[[Category: Kurisu G]]
-
[[Category: Minoura, I]]
+
[[Category: Minoura I]]
-
[[Category: Muto, E]]
+
[[Category: Muto E]]
-
[[Category: Namba, K]]
+
[[Category: Namba K]]
-
[[Category: Nishikawa, Y]]
+
[[Category: Nishikawa Y]]
-
[[Category: Sutoh, K]]
+
[[Category: Sutoh K]]
-
[[Category: Takazaki, H]]
+
[[Category: Takazaki H]]
-
[[Category: Uchimura, S]]
+
[[Category: Uchimura S]]
-
[[Category: Motor protein-cytoskeleton complex]]
+
-
[[Category: Motor protein-structural protein complex]]
+

Current revision

Pseudo-atomic model of dynein microtubule binding domain-tubulin complex based on a cryoEM map

3j6p, resolution 8.20Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3j6p"
Personal tools