Alpha-tubulin N-acetyltransferase

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<StructureSection load='3vwe' size='340' side='right' caption='Human α-tubulin N-acetyltransferase catalytic domain complex with CoA (PDB code [[3vwe]])' scene=''>
<StructureSection load='3vwe' size='340' side='right' caption='Human α-tubulin N-acetyltransferase catalytic domain complex with CoA (PDB code [[3vwe]])' scene=''>
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'''Alpha-tubulin N-acetyltransferase''' (TAT) catalyzes the conversion of acetyl-CoA and tubulin-L-lysine to CoA and tubulin-N-acetyl-L-lysine. TAT acetylates Lys40 in tubulin and is required for normal sperm flagellar function. This posttranslational modification of tubulin is conserved in long-lived microtubules. TAT can acetylate itself and this acts as a regulatory mechanism for its action on tubulin.
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'''Alpha-tubulin N-acetyltransferase''' (TAT) catalyzes the conversion of acetyl-CoA and tubulin-L-lysine to CoA and tubulin-N-acetyl-L-lysine. TAT acetylates Lys40 in tubulin and is required for normal sperm flagellar function. This posttranslational modification of tubulin is conserved in long-lived microtubules. TAT can acetylate itself and this acts as a regulatory mechanism for its action on tubulin.<ref>PMID:23071314</ref>
</StructureSection>
</StructureSection>

Revision as of 11:26, 3 December 2015

Human α-tubulin N-acetyltransferase catalytic domain complex with CoA (PDB code 3vwe)

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3D Structures of Alpha-tubulin N-acetyltransferase

Updated on 03-December-2015

4gs4, 4b5o, 4if5 – hTAT catalytic domain - human
4b5p – hTAT catalytic domain (mutant)
4h6z, 4yrh – zfTAT catalytic domain – zebra fish
4h6u – zfTAT catalytic domain (mutant)
4hkf – zfTAT catalytic domain + acetyl-CoA
3vwd – hTAT catalytic domain + acetoacetyl-CoA
3vwe – hTAT catalytic domain + CoA
4pk2, 4pk3 – hTAT catalytic domain + bisubstrate analog

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

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Michal Harel, Joel L. Sussman, Alexander Berchansky

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