5g0h

<StructureSection load='5g0h' size='340' side='right' caption='[[5g0h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[5g0h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G0H FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E1Z:S-TRICHOSTATIN+A'>E1Z</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g0f|5g0f]], [[5g0g|5g0g]], [[5g0i|5g0i]], [[5g0j|5g0j]]</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=5g0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g0h OCA], [http://pdbe.org/5g0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g0h RCSB], [http://www.ebi.ac.uk/pdbsum/5g0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g0h ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

We report crystal structures of zebrafish histone deacetylase 6 (HDAC6) catalytic domains in tandem or as single domains in complex with the (R) and (S) enantiomers of trichostatin A (TSA) or with the HDAC6-specific inhibitor nexturastat A. The tandem domains formed, together with the inter-domain linker, an ellipsoid-shaped complex with pseudo-twofold symmetry. We identified important active site differences between both catalytic domains and revealed the binding mode of HDAC6 selective inhibitors. HDAC inhibition assays with (R)- and (S)-TSA showed that (R)-TSA was a broad-range inhibitor, whereas (S)-TSA had moderate selectivity for HDAC6. We identified a uniquely positioned alpha-helix and a flexible tryptophan residue in the loop joining alpha-helices H20 to H21 as critical for deacetylation of the physiologic substrate tubulin. Using single-molecule measurements and biochemical assays we demonstrated that HDAC6 catalytic domain 2 deacetylated alpha-tubulin lysine 40 in the lumen of microtubules, but that its preferred substrate was unpolymerized tubulin.

 

== References ==

[[Category: Gut, H]]

[[Category: Helquist, P]]

[[Category: Hess, D]]

[[Category: Keusch, J J]]

[[Category: Matthias, P]]

[[Category: Melancon, B J]]

[[Category: Miyake, Y]]

[[Category: Saito, M]]

[[Category: Wang, L]]

[[Category: Wang, X]]

[[Category: Histone deacetylase]]