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| | ==tubulin acetyltransferase complex with bisubstrate analog== | | ==tubulin acetyltransferase complex with bisubstrate analog== |
| - | <StructureSection load='4pk2' size='340' side='right' caption='[[4pk2]], [[Resolution|resolution]] 1.35Å' scene=''> | + | <StructureSection load='4pk2' size='340' side='right'caption='[[4pk2]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pk2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PK2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pk2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PK2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PRK:N~6~-PROPANOYL-L-LYSINE'>PRK</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATAT1, C6orf134, MEC17, Nbla00487 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4pk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pk2 OCA], [https://pdbe.org/4pk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pk2 RCSB], [https://www.ebi.ac.uk/pdbsum/4pk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pk2 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-tubulin_N-acetyltransferase Alpha-tubulin N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.108 2.3.1.108] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pk2 OCA], [http://pdbe.org/4pk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pk2 RCSB], [http://www.ebi.ac.uk/pdbsum/4pk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pk2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATAT_HUMAN ATAT_HUMAN]] Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development.<ref>PMID:20829795</ref> | + | [https://www.uniprot.org/uniprot/ATAT_HUMAN ATAT_HUMAN] Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development.<ref>PMID:20829795</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4pk2" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4pk2" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Alpha-tubulin N-acetyltransferase 3D structures|Alpha-tubulin N-acetyltransferase 3D structures]] |
| | + | *[[Tubulin acetyltransferase|Tubulin acetyltransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-tubulin N-acetyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Roll-Mecak, A]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Szyk, A]] | + | [[Category: Roll-Mecak A]] |
| - | [[Category: Acetyltransferase]] | + | [[Category: Szyk A]] |
| - | [[Category: Bisubstrate]]
| + | |
| - | [[Category: Coa]]
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| - | [[Category: Transferase-peptide complex]]
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| - | [[Category: Tubulin]]
| + | |
| Structural highlights
Function
ATAT_HUMAN Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development.[1]
Publication Abstract from PubMed
Acetylation of alpha-tubulin Lys40 by tubulin acetyltransferase (TAT) is the only known posttranslational modification in the microtubule lumen. It marks stable microtubules and is required for polarity establishment and directional migration. Here, we elucidate the mechanistic underpinnings for TAT activity and its preference for microtubules with slow turnover. 1.35 A TAT cocrystal structures with bisubstrate analogs constrain TAT action to the microtubule lumen and reveal Lys40 engaged in a suboptimal active site. Assays with diverse tubulin polymers show that TAT is stimulated by microtubule interprotofilament contacts. Unexpectedly, despite the confined intraluminal location of Lys40, TAT efficiently scans the microtubule bidirectionally and acetylates stochastically without preference for ends. First-principles modeling and single-molecule measurements demonstrate that TAT catalytic activity, not constrained luminal diffusion, is rate limiting for acetylation. Thus, because of its preference for microtubules over free tubulin and its modest catalytic rate, TAT can function as a slow clock for microtubule lifetimes.
Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase.,Szyk A, Deaconescu AM, Spector J, Goodman B, Valenstein ML, Ziolkowska NE, Kormendi V, Grigorieff N, Roll-Mecak A Cell. 2014 Jun 5;157(6):1405-15. doi: 10.1016/j.cell.2014.03.061. PMID:24906155[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Akella JS, Wloga D, Kim J, Starostina NG, Lyons-Abbott S, Morrissette NS, Dougan ST, Kipreos ET, Gaertig J. MEC-17 is an alpha-tubulin acetyltransferase. Nature. 2010 Sep 9;467(7312):218-22. doi: 10.1038/nature09324. PMID:20829795 doi:10.1038/nature09324
- ↑ Szyk A, Deaconescu AM, Spector J, Goodman B, Valenstein ML, Ziolkowska NE, Kormendi V, Grigorieff N, Roll-Mecak A. Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase. Cell. 2014 Jun 5;157(6):1405-15. doi: 10.1016/j.cell.2014.03.061. PMID:24906155 doi:http://dx.doi.org/10.1016/j.cell.2014.03.061
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