8vt7

From Proteopedia

(Difference between revisions)

Current revision

Structure of the gamma tubulin ring complex nucleated microtubule protofilament.

Structural highlights

8vt7 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:	Electron Microscopy, Resolution 2.66Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

TBB3_HUMAN Congenital fibrosis of extraocular muscles;Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation. 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

TBB3_HUMAN 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. TUBB3 plays a critical role in proper axon guidance and mantainance.^[1]

Publication Abstract from PubMed

Microtubules are composed of alpha-tubulin and beta-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale alpha/beta-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa gamma-tubulin ring complex (gamma-TuRC), an essential regulator of microtubule formation that contains 14 gamma-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of gamma-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of gamma-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between gamma-tubulins and alpha-tubulins. Our structures suggest that gamma-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules.

, PMID:38609661^[2]

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

References

↑ Tischfield MA, Baris HN, Wu C, Rudolph G, Van Maldergem L, He W, Chan WM, Andrews C, Demer JL, Robertson RL, Mackey DA, Ruddle JB, Bird TD, Gottlob I, Pieh C, Traboulsi EI, Pomeroy SL, Hunter DG, Soul JS, Newlin A, Sabol LJ, Doherty EJ, de Uzcategui CE, de Uzcategui N, Collins ML, Sener EC, Wabbels B, Hellebrand H, Meitinger T, de Berardinis T, Magli A, Schiavi C, Pastore-Trossello M, Koc F, Wong AM, Levin AV, Geraghty MT, Descartes M, Flaherty M, Jamieson RV, Moller HU, Meuthen I, Callen DF, Kerwin J, Lindsay S, Meindl A, Gupta ML Jr, Pellman D, Engle EC. Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, and axon guidance. Cell. 2010 Jan 8;140(1):74-87. doi: 10.1016/j.cell.2009.12.011. PMID:20074521 doi:http://dx.doi.org/10.1016/j.cell.2009.12.011
↑ Aher A, Urnavicius L, Xue A, Neselu K, Kapoor TM. Structure of the γ-tubulin ring complex-capped microtubule. Nat Struct Mol Biol. 2024 Jul;31(7):1124-1133. PMID:38609661 doi:10.1038/s41594-024-01264-z

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8vt7"

Categories: Homo sapiens | Large Structures | Aher A | Kapoor TM | Urnavicius L

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8vt7 is ON HOLD
+==Structure of the gamma tubulin ring complex nucleated microtubule protofilament.==
+<StructureSection load='8vt7' size='340' side='right'caption='[[8vt7]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8vt7]] 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=8VT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VT7 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.66&#8491;</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></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=8vt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vt7 OCA], [https://pdbe.org/8vt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vt7 RCSB], [https://www.ebi.ac.uk/pdbsum/8vt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vt7 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/TBB3_HUMAN TBB3_HUMAN] Congenital fibrosis of extraocular muscles;Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation. 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 ==
+[https://www.uniprot.org/uniprot/TBB3_HUMAN TBB3_HUMAN] 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. TUBB3 plays a critical role in proper axon guidance and mantainance.<ref>PMID:20074521</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Microtubules are composed of alpha-tubulin and beta-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale alpha/beta-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa gamma-tubulin ring complex (gamma-TuRC), an essential regulator of microtubule formation that contains 14 gamma-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of gamma-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of gamma-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between gamma-tubulins and alpha-tubulins. Our structures suggest that gamma-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules.
-Authors:
+,  PMID:38609661<ref>PMID:38609661</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8vt7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Aher A]]
+[[Category: Kapoor TM]]
+[[Category: Urnavicius L]]

8vt7

From Proteopedia

Current revision

Structure of the gamma tubulin ring complex nucleated microtubule protofilament.

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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