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| | <StructureSection load='5g0y' size='340' side='right'caption='[[5g0y]], [[Resolution|resolution]] 2.29Å' scene=''> | | <StructureSection load='5g0y' size='340' side='right'caption='[[5g0y]], [[Resolution|resolution]] 2.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5g0y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G0Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5G0Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5g0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G0Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g0x|5g0x]], [[5g10|5g10]], [[5g11|5g11]], [[5g12|5g12]], [[5g13|5g13]], [[5g17|5g17]], [[5g1a|5g1a]], [[5g1b|5g1b]], [[5g1c|5g1c]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5g0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g0y OCA], [http://pdbe.org/5g0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g0y RCSB], [http://www.ebi.ac.uk/pdbsum/5g0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g0y 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=5g0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g0y OCA], [https://pdbe.org/5g0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g0y RCSB], [https://www.ebi.ac.uk/pdbsum/5g0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g0y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HDAH_PSEAE HDAH_PSEAE] Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines.<ref>PMID:26956223</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5g0y" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5g0y" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Kraemer, A]] | + | [[Category: Kraemer A]] |
| - | [[Category: Meyer-Almes, F J]] | + | [[Category: Meyer-Almes FJ]] |
| - | [[Category: Yildiz, O]] | + | [[Category: Yildiz O]] |
| - | [[Category: Hdac]]
| + | |
| - | [[Category: Hdah]]
| + | |
| - | [[Category: Hdlp]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
HDAH_PSEAE Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines.[1]
Publication Abstract from PubMed
Despite the recently growing interest in the acetylation of lysine residues by prokaryotic enzymes, the underlying biological function is still not well understood. Deacetylation is accomplished by proteins that belong to the histone deacetylase (HDAC) superfamily. In this report, we present the first crystal structure of PA3774, a histone deacetylase homologue from the human pathogen Pseudomonas aeruginosa that shares a high degree of homology with class IIb HDACs. We determined the crystal structure of the ligand-free enzyme and protein-ligand complexes with a trifluoromethylketone inhibitor and the reaction product acetate. Moreover, we produced loss of function mutants and determined the structure of the inhibitor-free PA3774H143A mutant, the inhibitor-free PA3774Y313F mutant, and the PA3774Y313F mutant in complex with the highly selective hydroxamate inhibitor PFSAHA. The overall structure reveals that the exceptionally long L1 loop mediates the formation of a tetramer composed of two "head-to-head" dimers. The distinctive dimer interface significantly confines the entrance area of the active site, suggesting a crucial role for substrate recognition and selectivity.
Crystal Structure of a Histone Deacetylase Homologue from Pseudomonas aeruginosa.,Kramer A, Wagner T, Yildiz O, Meyer-Almes FJ Biochemistry. 2016 Dec 13;55(49):6858-6868. Epub 2016 Nov 29. PMID:27951649[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Krämer A, Herzer J, Overhage J, Meyer-Almes FJ. Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa. BMC Biochem. 2016 Mar 9;17:4. PMID:26956223 doi:10.1186/s12858-016-0063-z
- ↑ Kramer A, Wagner T, Yildiz O, Meyer-Almes FJ. Crystal Structure of a Histone Deacetylase Homologue from Pseudomonas aeruginosa. Biochemistry. 2016 Dec 13;55(49):6858-6868. Epub 2016 Nov 29. PMID:27951649 doi:http://dx.doi.org/10.1021/acs.biochem.6b00613
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