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4b5o

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Revision as of 07:00, 31 August 2022

Crystal structure of human alpha tubulin acetyltransferase catalytic domain

Structural highlights

4b5o is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4b5p
Activity:	Alpha-tubulin N-acetyltransferase, with EC number 2.3.1.108
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4b5o"

@@ Line 3: / Line 3: @@
 <StructureSection load='4b5o' size='340' side='right'caption='[[4b5o]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4b5o]] is a 1 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=4B5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B5O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4b5o]] is a 1 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=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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b5p|4b5p]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b5p|4b5p]]</div></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>
+<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5o OCA], [http://pdbe.org/4b5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b5o RCSB], [http://www.ebi.ac.uk/pdbsum/4b5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b5o 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=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 ==
-[[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;">
 == Publication Abstract from PubMed ==

4b5o

From Proteopedia

Revision as of 07:00, 31 August 2022

Crystal structure of human alpha tubulin acetyltransferase catalytic domain

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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