Tubulin: Difference between revisions

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[[Image:1z5w.png|left|200px|thumb|Crystal Structure of Tubulin [[1z5w]]]]
<StructureSection load='' size='350' side='right' caption='γ-tubulin complex with GTP and Mg+2 ion (green), [[1z5w]]' scene='43/430888/Cv/2' pspeed='8'>
{{STRUCTURE_1z5w|  PDB=1z5w  | SIZE=300| SCENE=Tubulin/Cv/1 |right|CAPTION=Tubulin [[1z5w]] }}
== Function ==


[[Tubulin]] (TUB) is a constituent of microtubules in eukaryotes.  Microtubules are assembled from dimers of α-tubulin (TUBA) and β-tubulin (TUBB) bound to GTP. γ-tubulin (TUBG) is part of the nucleation of microtubules. Human TUB contains several numbered subtypes.  FtsZ  (Filamenting temperature-sensitive mutant Z) is a prokaryotic homologue of TUB. The images at the left and at the right correspond to one representative Tubulin, ''i.e.'' the crystal structure of Tubulin ([[1z5w]]).
[[Tubulin]] (TUB) is a constituent of microtubules in eukaryotes.  Microtubules are assembled from dimers of '''α-tubulin''' (TUBA) and '''β-tubulin''' (TUBB) bound to GTP. '''γ-tubulin''' (TUBG) is part of the nucleation of microtubules<ref>PMID:11297925</ref>. Human TUB contains several numbered subtypes.  Tubulin filaments are stabilized by taxol and zampanolide.  '''FtsZ''' (Filamenting temperature-sensitive mutant Z) is a prokaryotic homologue of TUB<ref>PMID:26463348</ref>. See [[Cell division protein]] and [[Beta tubulin]].


{{TOC limit|limit=2}}
== Relevance ==


== 3D Structures of Tubulin ==
The chemotherapeutic drug Taxol interacts with TUBB.  See [[Molecular Playground/Taxol]].  TUBA and TUBB expression in polyps of invasive colon cancer is different from normal<ref>PMID:16101133</ref>.


See [[Paclitaxel]].


=== Tubulin ===
== Disease ==
Mutations in TUBB underlie a large spectrum of neuronal migration disorders<ref>PMID:19465910</ref>.


[[3hkb]], [[3hkc]], [[3hkd]], [[3hke]], [[3n2g]], [[3n2k]] – TUBA+TUBB+stathmin-like protein B3 – sheep<br />
== Structural highlights ==
[[2wbe]] – cTUBA1D+cTUBB2B+kinesin+AMPPNP – cow<br />
*<scene name='43/430888/Cv/6'>γ-tubulin interactions with GTP and Mg+2 ion</scene> ([[1z5w]]).
[[3dco]] - cTUBA+cTUBB+kinesin-like NOD<br />
== 3D Structures of Tubulin ==
[[1tvk]] - cTUBA+cTUBB+GDP+GTP+Epothilone A – electron crystallography<br />
[[Tubulin 3D Structures]]
[[3iz0]] - cTUBA+cTUBB+hNDC80/SPC25+hNUF2/SPC24 – electron microscopy<br />
[[3edl]] - cTUBA1D+cTUBB2B+kinesin motor domain<br />
[[2xrp]] - cTUBA1D+cTUBB2B+doublecortin <br />
[[3du7]], [[3e22]], [[1z2b]], [[1sa0]], [[1sa1]] – cTUBA1C+cTUBB2B+stathmin-like protein B3<br />
[[1ffx]] - cTUBA+cTUBB+stathmin-like protein B3<br />
[[1jff]] - cTUBA+cTUBB<br />
[[2p4n]] - hTUBA+hTUBB+kinesin heavy chain<br />
[[3cb2]] – hTUBG1+GDP<br />
[[1z5v]] - hTUBG1+GTPgS<br />
[[1z5w]] - hTUBG1+GTP<br />
[[2hxf]] - pTUBA+pTUBB+kinesin-like KIF1A+AMPPNP – pig<br />
[[2hxh]] - pTUBA+pTUBB+kinesin-like KIF1A+ADP<br />
[[1ia0]] - pTUBA+pTUBB+kinesin-like KIF1A+ATP<br />
[[1tub]] - pTUBA+pTUBB – electron diffraction<br />
[[2bto]] – PdTUBA+thioredoxin 1 – ''Prosthecobacter dejongeii''<br />
[[2btq]] – PdTUBA+PdTUBB
 
 
=== FtsZ ===


[[2rhh]], [[2rhj]] – BsFtsZ+SO4 – ''Bacillus subtilis''<br />
</StructureSection>
[[2rhl]] - BsFtsZ+GDP<br />
[[2rho]] - BsFtsZ+GDP+GTP-gamma-S<br />
[[2vxy]], [[2vam]] – BsFtsZ<br />
[[2ve8]] – PaFtsZ gamma domain – ''Pseudomonas aeruginosa''<br />
[[2ve9]] - PaFtsZ gamma domain+DNA<br />
[[2vaw]] – PaFtsZ+GDP<br />
[[1ofu]] - PaFtsZ+SULA<br />
[[2r75]] - AaFtsZ+8-morpholino-GTP – ''Aquifex aeolicus''<br />
[[2r6r]] - AaFtsZ<br />
[[2q1x]], [[1rq2]] - MtFtsZ+citrate – ''Mycobacterium tuberculosis''<br />
[[2q1y]], [[1rlu]] - MtFtsZ+GTP-gamma-S<br />
[[1rq7]] - MtFtsZ+GDP<br />
[[2vap]] – MjFtsZ+GDP – ''Methancaldococcus jannaschii''<br />
[[1w58]] - MjFtsZ+GMPCPP<br />
[[1w59]], [[1fsz]] – MjFtsZ<br />
[[1w5a]] - MjFtsZ+MgGTP<br />
[[1w5b]] - MjFtsZ+GTP<br />
[[1w5e]], [[1w5f]] – MjFtsZ (mutant)


== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:32, 20 August 2024

Function

Tubulin (TUB) is a constituent of microtubules in eukaryotes. Microtubules are assembled from dimers of α-tubulin (TUBA) and β-tubulin (TUBB) bound to GTP. γ-tubulin (TUBG) is part of the nucleation of microtubules[1]. Human TUB contains several numbered subtypes. Tubulin filaments are stabilized by taxol and zampanolide. FtsZ (Filamenting temperature-sensitive mutant Z) is a prokaryotic homologue of TUB[2]. See Cell division protein and Beta tubulin.

Relevance

The chemotherapeutic drug Taxol interacts with TUBB. See Molecular Playground/Taxol. TUBA and TUBB expression in polyps of invasive colon cancer is different from normal[3].

See Paclitaxel.

Disease

Mutations in TUBB underlie a large spectrum of neuronal migration disorders[4].

Structural highlights

3D Structures of Tubulin

Tubulin 3D Structures


γ-tubulin complex with GTP and Mg+2 ion (green), 1z5w

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Moritz M, Agard DA. Gamma-tubulin complexes and microtubule nucleation. Curr Opin Struct Biol. 2001 Apr;11(2):174-81. PMID:11297925
  2. ↑ Arjes HA, Lai B, Emelue E, Steinbach A, Levin PA. Mutations in the bacterial cell division protein FtsZ highlight the role of GTP binding and longitudinal subunit interactions in assembly and function. BMC Microbiol. 2015 Oct 13;15:209. doi: 10.1186/s12866-015-0544-z. PMID:26463348 doi:http://dx.doi.org/10.1186/s12866-015-0544-z
  3. ↑ Giarnieri E, De Francesco GP, Carico E, Midiri G, Amanti C, Giacomelli L, Tucci G, Gidaro S, Stroppa I, Gidaro G, Giovagnoli MR. Alpha- and beta-tubulin expression in rectal cancer development. Anticancer Res. 2005 Sep-Oct;25(5):3237-41. PMID:16101133
  4. ↑ Jaglin XH, Poirier K, Saillour Y, Buhler E, Tian G, Bahi-Buisson N, Fallet-Bianco C, Phan-Dinh-Tuy F, Kong XP, Bomont P, Castelnau-Ptakhine L, Odent S, Loget P, Kossorotoff M, Snoeck I, Plessis G, Parent P, Beldjord C, Cardoso C, Represa A, Flint J, Keays DA, Cowan NJ, Chelly J. Mutations in the beta-tubulin gene TUBB2B result in asymmetrical polymicrogyria. Nat Genet. 2009 Jun;41(6):746-52. doi: 10.1038/ng.380. Epub 2009 May 24. PMID:19465910 doi:http://dx.doi.org/10.1038/ng.380

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Alexander Berchansky, Michal Harel, Joel L. Sussman
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