3jat

From Proteopedia

(Difference between revisions)

Revision as of 13:30, 4 May 2022

Cryo-EM structure of GMPCPP-microtubule (14 protofilaments) decorated with kinesin

3jat, resolution 3.50Å

Structural highlights

3jat is a 12 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3jak, 3jal, 3jar, 3jas
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. [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.

Publication Abstract from PubMed

Microtubule (MT) dynamic instability is driven by GTP hydrolysis and regulated by microtubule-associated proteins, including the plus-end tracking end-binding protein (EB) family. We report six cryo-electron microscopy (cryo-EM) structures of MTs, at 3.5 A or better resolution, bound to GMPCPP, GTPgammaS, or GDP, either decorated with kinesin motor domain after polymerization or copolymerized with EB3. Subtle changes around the E-site nucleotide during hydrolysis trigger conformational changes in alpha-tubulin around an "anchor point," leading to global lattice rearrangements and strain generation. Unlike the extended lattice of the GMPCPP-MT, the EB3-bound GTPgammaS-MT has a compacted lattice that differs in lattice twist from that of the also compacted GDP-MT. These results and the observation that EB3 promotes rapid hydrolysis of GMPCPP suggest that EB proteins modulate structural transitions at growing MT ends by recognizing and promoting an intermediate state generated during GTP hydrolysis. Our findings explain both EBs end-tracking behavior and their effect on microtubule dynamics.

Mechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins.,Zhang R, Alushin GM, Brown A, Nogales E Cell. 2015 Jul 28. pii: S0092-8674(15)00849-1. doi: 10.1016/j.cell.2015.07.012. PMID:26234155^[1]

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

References

↑ Zhang R, Alushin GM, Brown A, Nogales E. Mechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins. Cell. 2015 Jul 28. pii: S0092-8674(15)00849-1. doi: 10.1016/j.cell.2015.07.012. PMID:26234155 doi:http://dx.doi.org/10.1016/j.cell.2015.07.012

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/3jat"

@@ Line 3: / Line 3: @@
 <SX load='3jat' size='340' side='right' viewer='molstar' caption='[[3jat]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3jat]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JAT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JAT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3jat]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JAT 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></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jak|3jak]], [[3jal|3jal]], [[3jar|3jar]], [[3jas|3jas]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jak|3jak]], [[3jal|3jal]], [[3jar|3jar]], [[3jas|3jas]]</div></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=3jat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jat OCA], [http://pdbe.org/3jat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jat RCSB], [http://www.ebi.ac.uk/pdbsum/3jat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jat 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=3jat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jat OCA], [https://pdbe.org/3jat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jat RCSB], [https://www.ebi.ac.uk/pdbsum/3jat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jat 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. [[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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3jat

From Proteopedia

Revision as of 13:30, 4 May 2022

Cryo-EM structure of GMPCPP-microtubule (14 protofilaments) decorated with kinesin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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