4if5: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 4if5~~ is ~~ON HOLD until Jun 13 2015~~

==Structure of human Mec17==

== Structural highlights ==

<table><tr><td colspan='2'>[[4if5]] 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=4IF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IF5 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]] 1.7Å</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4if5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4if5 OCA], [https://pdbe.org/4if5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4if5 RCSB], [https://www.ebi.ac.uk/pdbsum/4if5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4if5 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>

== Publication Abstract from PubMed ==

Tubulin protomers undergo an extensive array of post-translational modifications to tailor microtubules to specific tasks. One such modification, the acetylation of lysine 40 of alpha-tubulin, located in the lumen of microtubules, is associated with stable, long-living microtubule structures. MEC-17 was recently identified as the acetyltransferase that mediates this event. We have determined the crystal structure of the catalytic core of human MEC-17 in complex with its cofactor acetyl-CoA at 1.7A resolution. The structure reveals that the MEC-17 core adopts a canonical Gcn5-related N-acetyltransferase (GNAT) fold that is decorated with extensive surface loops. An enzymatic analysis of 33 MEC-17 surface mutants identifies hot-spot residues for catalysis and substrate recognition. A large, evolutionarily conserved hydrophobic surface patch that is critical for enzymatic activity is identified, suggesting that specificity is achieved by interactions with the alpha-tubulin substrate that extend outside of the modified surface loop. An analysis of MEC-17 mutants in Caenorhabditis elegans shows that enzymatic activity is dispensable for touch sensitivity.

~~Authors:~~ Davenport~~, A.M.~~, Collins, L., Minor~~, P.~~, Sternberg, P., ~~Hoelz, A~~.

Structural and Functional Characterization of the alpha-Tubulin Acetyltransferase MEC-17.,Davenport AM, Collins LN, Chiu H, Minor PJ, Sternberg PW, Hoelz A J Mol Biol. 2014 Jul 15;426(14):2605-16. doi: 10.1016/j.jmb.2014.05.009. Epub, 2014 May 17. PMID:24846647<ref>PMID:24846647</ref>

~~Description~~: ~~Structure of human Mec17~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Alpha-tubulin N-acetyltransferase 3D structures|Alpha-tubulin N-acetyltransferase 3D structures]]

*[[Tubulin acetyltransferase|Tubulin acetyltransferase]]

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Collins L]]

[[Category: Davenport AM]]

[[Category: Hoelz A]]

[[Category: Minor P]]

[[Category: Sternberg P]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4if5 is ON HOLD  until Jun 13 2015
+==Structure of human Mec17==
+<StructureSection load='4if5' size='340' side='right'caption='[[4if5]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4if5]] 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=4IF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IF5 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]] 1.7&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4if5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4if5 OCA], [https://pdbe.org/4if5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4if5 RCSB], [https://www.ebi.ac.uk/pdbsum/4if5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4if5 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 ==
+Tubulin protomers undergo an extensive array of post-translational modifications to tailor microtubules to specific tasks. One such modification, the acetylation of lysine 40 of alpha-tubulin, located in the lumen of microtubules, is associated with stable, long-living microtubule structures. MEC-17 was recently identified as the acetyltransferase that mediates this event. We have determined the crystal structure of the catalytic core of human MEC-17 in complex with its cofactor acetyl-CoA at 1.7A resolution. The structure reveals that the MEC-17 core adopts a canonical Gcn5-related N-acetyltransferase (GNAT) fold that is decorated with extensive surface loops. An enzymatic analysis of 33 MEC-17 surface mutants identifies hot-spot residues for catalysis and substrate recognition. A large, evolutionarily conserved hydrophobic surface patch that is critical for enzymatic activity is identified, suggesting that specificity is achieved by interactions with the alpha-tubulin substrate that extend outside of the modified surface loop. An analysis of MEC-17 mutants in Caenorhabditis elegans shows that enzymatic activity is dispensable for touch sensitivity.
-Authors: Davenport, A.M., Collins, L., Minor, P., Sternberg, P., Hoelz, A.
+Structural and Functional Characterization of the alpha-Tubulin Acetyltransferase MEC-17.,Davenport AM, Collins LN, Chiu H, Minor PJ, Sternberg PW, Hoelz A J Mol Biol. 2014 Jul 15;426(14):2605-16. doi: 10.1016/j.jmb.2014.05.009. Epub, 2014 May 17. PMID:24846647<ref>PMID:24846647</ref>
-Description: Structure of human Mec17
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4if5" 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: Collins L]]
+[[Category: Davenport AM]]
+[[Category: Hoelz A]]
+[[Category: Minor P]]
+[[Category: Sternberg P]]