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| | ==Crystal structure of protein acetyltransferase (PAT) from Sulfolobus solfataricus== | | ==Crystal structure of protein acetyltransferase (PAT) from Sulfolobus solfataricus== |
| - | <StructureSection load='3f8k' size='340' side='right' caption='[[3f8k]], [[Resolution|resolution]] 1.84Å' scene=''> | + | <StructureSection load='3f8k' size='340' side='right'caption='[[3f8k]], [[Resolution|resolution]] 1.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3f8k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulso Sulso]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F8K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3f8k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F8K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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]] 1.84Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSO2813 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SULSO])</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=3f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f8k OCA], [https://pdbe.org/3f8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f8k RCSB], [https://www.ebi.ac.uk/pdbsum/3f8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f8k ProSAT]</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=3f8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f8k OCA], [http://pdbe.org/3f8k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f8k RCSB], [http://www.ebi.ac.uk/pdbsum/3f8k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f8k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAT_SACS2 PAT_SACS2] Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.<ref>PMID:15824122</ref> <ref>PMID:19473964</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f8/3f8k_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f8/3f8k_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Sulso]] | + | [[Category: Large Structures]] |
| - | [[Category: Brent, M M]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Gcn5-related n-acetyltransferase]] | + | [[Category: Brent MM]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PAT_SACS2 Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Sulfolobus solfataricus protein acetyltransferase (PAT) acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys(16) to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a "primitive" model for chromatin regulation analogous to histone modification in eukaryotes. We report the 1.84-A crystal structure of PAT in complex with coenzyme A. The structure reveals homology to both prokaryotic GNAT acetyltransferases and eukaryotic histone acetyltransferases (HATs), with an additional "bent helix" proximal to the substrate binding site that might play an autoregulatory function. Investigation of active site mutants suggests that PAT does not use a single general base or acid residue for substrate deprotonation and product reprotonation, respectively, and that a diffusional step, such as substrate binding, may be rate-limiting. The catalytic efficiency of PAT toward ALBA is low relative to other acetyltransferases, suggesting that there may be better, unidentified substrates for PAT. The structural similarity of PAT to eukaryotic HATs combined with its conserved role in chromatin regulation suggests that PAT is evolutionarily related to the eukaryotic HATs.
Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus.,Brent MM, Iwata A, Carten J, Zhao K, Marmorstein R J Biol Chem. 2009 Jul 17;284(29):19412-9. Epub 2009 May 27. PMID:19473964[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marsh VL, Peak-Chew SY, Bell SD. Sir2 and the acetyltransferase, Pat, regulate the archaeal chromatin protein, Alba. J Biol Chem. 2005 Jun 3;280(22):21122-8. PMID:15824122 doi:10.1074/jbc.M501280200
- ↑ Brent MM, Iwata A, Carten J, Zhao K, Marmorstein R. Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus. J Biol Chem. 2009 Jul 17;284(29):19412-9. Epub 2009 May 27. PMID:19473964 doi:10.1074/jbc.M109.014951
- ↑ Brent MM, Iwata A, Carten J, Zhao K, Marmorstein R. Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus. J Biol Chem. 2009 Jul 17;284(29):19412-9. Epub 2009 May 27. PMID:19473964 doi:10.1074/jbc.M109.014951
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