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[[Image:1zz0.gif|left|200px]]


{{Structure
==Crystal structure of a HDAC-like protein with acetate bound==
|PDB= 1zz0 |SIZE=350|CAPTION= <scene name='initialview01'>1zz0</scene>, resolution 1.60&Aring;
<StructureSection load='1zz0' size='340' side='right'caption='[[1zz0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[1zz0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenaceae_bacterium_FB188 Alcaligenaceae bacterium FB188]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZZ0 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zz0 OCA], [https://pdbe.org/1zz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zz0 RCSB], [https://www.ebi.ac.uk/pdbsum/1zz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zz0 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1zz1|1ZZ1]], [[1zz3|1ZZ3]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zz0 OCA], [http://www.ebi.ac.uk/pdbsum/1zz0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zz0 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/HDAH_ALCSD HDAH_ALCSD]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zz/1zz0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zz0 ConSurf].
<div style="clear:both"></div>


'''Crystal structure of a HDAC-like protein with acetate bound'''
==See Also==
 
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Histone deacetylases (HDACs) are among the most promising targets in cancer therapy. However, structural information greatly enhancing the design of HDAC inhibitors as novel chemotherapeutics has not been available on class 2 HDACs so far. Here we present the structure of the bacterial FB188 HDAH (histone deacetylase-like amidohydrolase from Bordetella/Alcaligenes strain FB188) that reveals high sequential and functional homology to human class 2 HDACs. FB188 HDAH is capable to remove the acetyl moiety from acetylated histones. Several HDAC-specific inhibitors, which have been shown to inhibit tumor activity in both pre-clinical models and in clinical trials, also inhibit FB188 HDAH. We have determined the crystal structure of FB188 HDAH at a resolution of 1.6 angstroms in complex with the reaction product acetate, as well as in complex with the inhibitors suberoylanilide hydroxamic acid (SAHA) and cyclopentyle-propionyle hydroxamic acid (CypX) at a resolution of 1.57 angstroms and 1.75 angstroms, respectively. FB188 HDAH exhibits the canonical fold of class 1 HDACs and contains a catalytic zinc ion. The highest structural diversity compared to class 1 enzymes is found in loop regions especially in the area around the entrance of the active site, indicating significant differences among the acetylated proteins binding to class 1 and 2 HDACs, respectively.
[[Category: Alcaligenaceae bacterium FB188]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Dickmanns A]]
1ZZ0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_sp. Bordetella sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZ0 OCA].
[[Category: Ficner R]]
 
[[Category: Hildmann C]]
==Reference==
[[Category: Nielsen TK]]
Crystal structure of a bacterial class 2 histone deacetylase homologue., Nielsen TK, Hildmann C, Dickmanns A, Schwienhorst A, Ficner R, J Mol Biol. 2005 Nov 18;354(1):107-20. Epub 2005 Oct 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16242151 16242151]
[[Category: Schwienhorst A]]
[[Category: Bordetella sp.]]
[[Category: Single protein]]
[[Category: Dickmanns, A.]]
[[Category: Ficner, R.]]
[[Category: Hildmann, C.]]
[[Category: Nielsen, T K.]]
[[Category: Schwienhorst, A.]]
[[Category: hydrolase]]
 
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