4b5p
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant== | |
| - | + | <StructureSection load='4b5p' size='340' side='right' caption='[[4b5p]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4b5p]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B5P FirstGlance]. <br> | |
| - | ==Function== | + | </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> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b5o|4b5o]]</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='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=4b5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b5p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b5p RCSB], [http://www.ebi.ac.uk/pdbsum/4b5p PDBsum]</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> | [[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> | ||
| + | <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> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Alpha-tubulin N-acetyltransferase]] | [[Category: Alpha-tubulin N-acetyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Lorentzen, E | + | [[Category: Lorentzen, E]] |
| - | [[Category: Taschner, M | + | [[Category: Taschner, M]] |
| - | [[Category: Vetter, M | + | [[Category: Vetter, M]] |
[[Category: Acetyl coa]] | [[Category: Acetyl coa]] | ||
[[Category: Cilium]] | [[Category: Cilium]] | ||
Revision as of 10:45, 25 December 2014
Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant
| |||||||||||
