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3j6h

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Revision as of 14:16, 24 January 2024

Nucleotide-free Kinesin motor domain complexed with GMPCPP-microtubule

3j6h, resolution 8.10Å

Structural highlights

3j6h 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 8.1Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Publication Abstract from PubMed

The molecular motor kinesin moves along microtubules using energy from ATP hydrolysis in an initial step coupled with ADP release. In neurons, kinesin-1/KIF5C preferentially binds to the GTP-state microtubules over GDP-state microtubules to selectively enter an axon among many processes; however, because the atomic structure of nucleotide-free KIF5C is unavailable, its molecular mechanism remains unresolved. Here, the crystal structure of nucleotide-free KIF5C and the cryo-electron microscopic structure of nucleotide-free KIF5C complexed with the GTP-state microtubule are presented. The structures illustrate mutual conformational changes induced by interaction between the GTP-state microtubule and KIF5C. KIF5C acquires the 'rigor conformation', where mobile switches I and II are stabilized through L11 and the initial portion of the neck-linker, facilitating effective ADP release and the weak-to-strong transition of KIF5C microtubule affinity. Conformational changes to tubulin strengthen the longitudinal contacts of the GTP-state microtubule in a similar manner to GDP-taxol microtubules. These results and functional analyses provide the molecular mechanism of the preferential binding of KIF5C to GTP-state microtubules.

X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding.,Morikawa M, Yajima H, Nitta R, Inoue S, Ogura T, Sato C, Hirokawa N EMBO J. 2015 Mar 16. pii: e201490588. PMID:25777528^[1]

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

References

↑ Morikawa M, Yajima H, Nitta R, Inoue S, Ogura T, Sato C, Hirokawa N. X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding. EMBO J. 2015 Mar 16. pii: e201490588. PMID:25777528 doi:http://dx.doi.org/10.15252/embj.201490588

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/3j6h"

@@ Line 3: / Line 3: @@
 <SX load='3j6h' size='340' side='right' viewer='molstar' caption='[[3j6h]], [[Resolution|resolution]] 8.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3j6h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] 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=3J6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J6H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3j6h]] 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=3J6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J6H FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 8.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kif5c ([https://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=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3j6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6h OCA], [https://pdbe.org/3j6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j6h RCSB], [https://www.ebi.ac.uk/pdbsum/3j6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j6h ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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/KIF5C_MOUSE KIF5C_MOUSE]] Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs.<ref>PMID:19608740</ref>  [[https://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/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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 28: / Line 28: @@
 </SX>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
 [[Category: Sus scrofa]]
-[[Category: Hirokawa, N]]
+[[Category: Hirokawa N]]
-[[Category: Inoue, S]]
+[[Category: Inoue S]]
-[[Category: Morikawa, M]]
+[[Category: Morikawa M]]
-[[Category: Nitta, R]]
+[[Category: Nitta R]]
-[[Category: Ogura, T]]
+[[Category: Ogura T]]
-[[Category: Sato, C]]
+[[Category: Sato C]]
-[[Category: Yajima, H]]
+[[Category: Yajima H]]
-[[Category: Axonal transport]]
-[[Category: Gmpcpp-microtubule]]
-[[Category: Kinesin]]
-[[Category: Microtubule]]
-[[Category: Motor domain]]
-[[Category: Nucleotide-free kinesin]]
-[[Category: Rigor-conformation]]
-[[Category: Structural protein-motor protein complex]]
-[[Category: Tubulin]]

3j6h

From Proteopedia

Revision as of 14:16, 24 January 2024

Nucleotide-free Kinesin motor domain complexed with GMPCPP-microtubule

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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