4b5o: Difference between revisions
New page: '''Unreleased structure''' The entry 4b5o is ON HOLD until Paper Publication Authors: Taschner, M., Vetter, M., Lorentzen, E. Description: Crystal structure of human alpha tubulin acet... |
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==Crystal structure of human alpha tubulin acetyltransferase catalytic domain== | |||
<StructureSection load='4b5o' size='340' side='right'caption='[[4b5o]], [[Resolution|resolution]] 1.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b5o]] is a 1 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=4B5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B5O 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]] 1.05Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5o OCA], [https://pdbe.org/4b5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b5o RCSB], [https://www.ebi.ac.uk/pdbsum/4b5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b5o ProSAT]</span></td></tr> | |||
</table> | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23071318</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4b5o" 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: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Lorentzen E]] | |||
[[Category: Taschner M]] | |||
[[Category: Vetter M]] | |||
Latest revision as of 13:57, 9 May 2024
Crystal structure of human alpha tubulin acetyltransferase catalytic domainCrystal structure of human alpha tubulin acetyltransferase catalytic domain
Structural highlights
FunctionATAT_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 PubMedAcetylation 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 AlsoReferences
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