Tubulin acetyltransferase

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== Function ==
== Function ==
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'''Tubulin acetyltransferase''' (TAT) is the major tubulin lysine-40 (K40) acetyltransferase. The posttranslational modification of tubulin is essential for stable, long-lived micrutubules<ref>PMID:23071314</ref>. This tubulin modification is conserved from prosits to humans. TAT accelerates microtubules dynamics via a mechanism distinct from acetylation<ref>PMID:23275437</ref>.
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'''Tubulin acetyltransferase''' or '''alpha-tubulin N-acetyltransferase''' (TAT) is the major tubulin lysine-40 (K40) acetyltransferase. TAT catalyzes the conversion of acetyl-CoA and tubulin-L-lysine to CoA and tubulin-N-acetyl-L-lysine. The posttranslational modification of tubulin is essential for stable, long-lived micrutubules<ref>PMID:23071314</ref>. This tubulin modification is conserved from prosits to humans. TAT accelerates microtubules dynamics via a mechanism distinct from acetylation<ref>PMID:23275437</ref>.
== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
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The <scene name='80/801769/Cv/7'>acetyl-CoA donor is encapsulated in a highly conserved basic pocket on the surface</scene> of TAT <scene name='80/801769/Cv/5'>forming numerous hydrogen bonds with TAT residues</scene>. Water moleculres are shown as red spheres. The <scene name='80/801769/Cv/6'>donor acetyl group is oriented by a hydrogen bond with the backbone of F124</scene> (colored in magenta) and is proximal to a groove which must bind the incoming K40 substrate of tubulin<ref>PMID:24846647</ref>.
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The <scene name='80/801769/Cv/8'>acetyl-CoA donor is encapsulated in a highly conserved basic pocket on the surface</scene> of TAT <scene name='80/801769/Cv/9'>forming numerous hydrogen bonds with TAT residues</scene>. Water moleculres are shown as red spheres. The <scene name='80/801769/Cv/10'>donor acetyl group is oriented by a hydrogen bond with the backbone of F124</scene> (colored in magenta) and is proximal to a groove which must bind the incoming K40 substrate of tubulin<ref>PMID:24846647</ref>.
</StructureSection>
</StructureSection>
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[4h6z]], [[4hkf]], [[4yrh] – zTAT + Acetyl CoA – zebrafish<br />
 
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[[4h6u]] – zTAT (mutant) + Acetyl CoA <br />
 
[[4pk2]], [[4pk3]] – hTAT catalytic domain + Acetyl CoA + bisubstrate analog - human<br />
[[4pk2]], [[4pk3]] – hTAT catalytic domain + Acetyl CoA + bisubstrate analog - human<br />
[[4gs4]], [[4b5o]], [[4u9y]], [[4u9z]], [[3vwe]], [[4if5]] – hTAT catalytic domain + Acetyl CoA <br />
[[4gs4]], [[4b5o]], [[4u9y]], [[4u9z]], [[3vwe]], [[4if5]] – hTAT catalytic domain + Acetyl CoA <br />
[[4b5p]] – hTAT catalytic domain (mutant) + Acetyl CoA <br />
[[4b5p]] – hTAT catalytic domain (mutant) + Acetyl CoA <br />
[[3vwd]] – hTAT catalytic domain + acetoacetyl CoA <br />
[[3vwd]] – hTAT catalytic domain + acetoacetyl CoA <br />
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[[4h6z]], [[4hkf]], [[4yrh]] – zTAT + Acetyl CoA – zebrafish<br />
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[[4h6u]] – zTAT (mutant) + Acetyl CoA <br />
== References ==
== References ==

Current revision

Se-Met human tubulin cetyltransferase complex with acetyl CoA and Cl- ion (green) (PDB code 4if5)

Drag the structure with the mouse to rotate

3D structures of tubulin acetyltransferase

Updated on 23-December-2020

4pk2, 4pk3 – hTAT catalytic domain + Acetyl CoA + bisubstrate analog - human
4gs4, 4b5o, 4u9y, 4u9z, 3vwe, 4if5 – hTAT catalytic domain + Acetyl CoA
4b5p – hTAT catalytic domain (mutant) + Acetyl CoA
3vwd – hTAT catalytic domain + acetoacetyl CoA
4h6z, 4hkf, 4yrh – zTAT + Acetyl CoA – zebrafish
4h6u – zTAT (mutant) + Acetyl CoA

References

  1. ↑ Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R. Structure of the alpha-tubulin acetyltransferase, alphaTAT1, and implications for tubulin-specific acetylation. Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19655-60. doi:, 10.1073/pnas.1209357109. Epub 2012 Oct 15. PMID:23071314 doi:10.1073/pnas.1209357109
  2. ↑ Kalebic N, Martinez C, Perlas E, Hublitz P, Bilbao-Cortes D, Fiedorczuk K, Andolfo A, Heppenstall PA. Tubulin acetyltransferase alphaTAT1 destabilizes microtubules independently of its acetylation activity. Mol Cell Biol. 2013 Mar;33(6):1114-23. doi: 10.1128/MCB.01044-12. Epub 2012 Dec, 28. PMID:23275437 doi:http://dx.doi.org/10.1128/MCB.01044-12
  3. ↑ Press ER, Shao Q, Kelly JJ, Chin K, Alaga A, Laird DW. Induction of cell death and gain-of-function properties of connexin26 mutants predict severity of skin disorders and hearing loss. J Biol Chem. 2017 Jun 9;292(23):9721-9732. doi: 10.1074/jbc.M116.770917. Epub, 2017 Apr 20. PMID:28428247 doi:http://dx.doi.org/10.1074/jbc.M116.770917
  4. ↑ Li L, Yang XJ. Tubulin acetylation: responsible enzymes, biological functions and human diseases. Cell Mol Life Sci. 2015 Nov;72(22):4237-55. doi: 10.1007/s00018-015-2000-5. Epub , 2015 Jul 31. PMID:26227334 doi:http://dx.doi.org/10.1007/s00018-015-2000-5
  5. ↑ Davenport AM, Collins LN, Chiu H, Minor PJ, Sternberg PW, Hoelz A. Structural and Functional Characterization of the alpha-Tubulin Acetyltransferase MEC-17. J Mol Biol. 2014 Jul 15;426(14):2605-16. doi: 10.1016/j.jmb.2014.05.009. Epub, 2014 May 17. PMID:24846647 doi:http://dx.doi.org/10.1016/j.jmb.2014.05.009

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