|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4b5p' size='340' side='right'caption='[[4b5p]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4b5p' size='340' side='right'caption='[[4b5p]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b5p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B5P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b5p]] is a 2 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=4B5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B5P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b5o|4b5o]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-tubulin_N-acetyltransferase Alpha-tubulin N-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.108 2.3.1.108] </span></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=4b5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5p OCA], [https://pdbe.org/4b5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b5p RCSB], [https://www.ebi.ac.uk/pdbsum/4b5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b5p ProSAT]</span></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=4b5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5p OCA], [https://pdbe.org/4b5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b5p RCSB], [https://www.ebi.ac.uk/pdbsum/4b5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b5p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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 == |
| Line 28: |
Line 27: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-tubulin N-acetyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lorentzen, E]] | + | [[Category: Lorentzen E]] |
| - | [[Category: Taschner, M]] | + | [[Category: Taschner M]] |
| - | [[Category: Vetter, M]] | + | [[Category: Vetter M]] |
| - | [[Category: Acetyl coa]]
| + | |
| - | [[Category: Cilium]]
| + | |
| - | [[Category: Intraflagellar transport]]
| + | |
| - | [[Category: Lysine acetyltransferase]]
| + | |
| - | [[Category: Microtubule]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[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 lysine residues is an important posttranslational modification found in all domains of life. alpha-tubulin is specifically acetylated on lysine 40, a modification that serves to stabilize microtubules of axons and cilia. Whereas histone acetyltransferases have been extensively studied, there is no structural and mechanistic information available on alpha-tubulin acetyltransferases. Here, we present the structure of the human alpha-tubulin acetyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at 1.05 A resolution. Compared with other lysine acetyltransferases of known structure, alpha-tubulin acetyltransferase displays a relatively well-conserved cosubstrate binding pocket but is unique in its active site and putative alpha-tubulin binding site. Using acetylation assays with structure-guided mutants, we map residues important for acetyl-CoA binding, substrate binding, and catalysis. This analysis reveals a basic patch implicated in substrate binding and a conserved glutamine residue required for catalysis, demonstrating that the family of alpha-tubulin acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases characterized to date.
Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA.,Taschner M, Vetter M, Lorentzen E Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19649-54. doi:, 10.1073/pnas.1209343109. Epub 2012 Oct 15. PMID:23071318[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
- ↑ Taschner M, Vetter M, Lorentzen E. Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA. Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19649-54. doi:, 10.1073/pnas.1209343109. Epub 2012 Oct 15. PMID:23071318 doi:10.1073/pnas.1209343109
|
