View source for 4h6u


==Tubulin acetyltransferase mutant==
<StructureSection load='4h6u' size='340' side='right'caption='[[4h6u]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4h6u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H6U FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4482&#8491;</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4h6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h6u OCA], [https://pdbe.org/4h6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h6u RCSB], [https://www.ebi.ac.uk/pdbsum/4h6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h6u ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATAT_DANRE ATAT_DANRE] Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. May promote directional cell locomotion and chemotaxis (By similarity). May be required for normal sperm flagellar function (By similarity). May affect microtubule stability and regulate microtubule dynamics. May be involved in neuron development. Acetylates alpha-tubulin in neurons, but not in cilia.[HAMAP-Rule:MF_03130]<ref>PMID:20829795</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tubulin acetyltransferase (TAT) acetylates Lys-40 of alpha-tubulin in the microtubule lumen. TAT is inefficient and its activity is enhanced when tubulin is incorporated in microtubules. Acetylation is associated with stable microtubules and regulates the binding of microtubule motors and associated proteins. TAT is important in neuronal polarity and mechanosensation and decreased tubulin acetylation levels are associated with axonal transport defects and neurodegeneration. We present the first structure of TAT in complex with ac-CoA at 2.7A resolution. The structure reveals a conserved stable catalytic core shared with other GCN5 superfamily acetyltransferases consisting of a central beta-sheet flanked by alpha-helices, and a C-terminal beta-hairpin unique to TAT. Structure-guided mutagenesis establishes the molecular determinants for ac-CoA and tubulin substrate recognition. The wild-type TAT construct is a monomer in solution. We identify a metastable interface between the conserved core and N-terminal domain that modulates the oligomerization of TAT in solution and is essential for activity. The 2.45A resolution structure of an inactive TAT construct with an active site point mutation near this interface reveals a domain swapped dimer in which the functionally essential N-terminus shows evidence of marked structural plasticity. The sequence segment corresponding to this structurally plastic region in TAT has been implicated in substrate recognition in other GCN5 superfamily acetyltransferases. Our structures provide a rational platform for the mechanistic dissection of TAT activity and the design of TAT inhibitors with therapeutic potential in neuronal regeneration.

Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N-terminus.,Kormendi V, Szyk A, Piszczek G, Roll-Mecak A J Biol Chem. 2012 Oct 26. PMID:23105108<ref>PMID:23105108</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4h6u" 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/>
__TOC__
</StructureSection>
[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Kizub V]]
[[Category: Roll-Mecak A]]
[[Category: Szyk A]]