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| | ==Crystal structure of paia n-acetyltransferase from thermoplasma acidophilum in complex with coenzyme a== | | ==Crystal structure of paia n-acetyltransferase from thermoplasma acidophilum in complex with coenzyme a== |
| - | <StructureSection load='3ne7' size='340' side='right' caption='[[3ne7]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3ne7' size='340' side='right'caption='[[3ne7]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ne7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NE7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ne7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NE7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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]] 2.3Å</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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f0a|3f0a]], [[3fix|3fix]], [[3k9u|3k9u]]</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=3ne7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne7 OCA], [https://pdbe.org/3ne7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ne7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ne7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne7 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ta0374 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</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=3ne7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ne7 OCA], [http://pdbe.org/3ne7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ne7 RCSB], [http://www.ebi.ac.uk/pdbsum/3ne7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ne7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAIA_THEAC PAIA_THEAC] Involved in the protection against polyamine toxicity by regulating their concentration. Could also be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine.<ref>PMID:21633970</ref> <ref>PMID:23184347</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/ne/3ne7_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/3ne7_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anderson, F W]] | + | [[Category: Large Structures]] |
| - | [[Category: Clancy, S]] | + | [[Category: Thermoplasma acidophilum]] |
| - | [[Category: Filippova, E V]] | + | [[Category: Anderson FW]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Clancy S]] |
| - | [[Category: Kiryukhina, O]] | + | [[Category: Filippova EV]] |
| - | [[Category: Structural genomic]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Minasov, G]] | + | [[Category: Kiryukhina O]] |
| - | [[Category: Shuvalova, L]] | + | [[Category: Minasov G]] |
| - | [[Category: Coenzyme some]] | + | [[Category: Shuvalova L]] |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
3ne7 is a 1 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PAIA_THEAC Involved in the protection against polyamine toxicity by regulating their concentration. Could also be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine.[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
GCN5-related N-acetyltransferases (GNATs) are the most widely distributed acetyltransferase systems among all three domains of life. GNATs appear to be involved in several key processes, including microbial antibiotic resistance, compacting eukaryotic DNA, controlling gene expression, and protein synthesis. Here, we report the crystal structure of a putative GNAT Ta0374 from Thermoplasma acidophilum, a hyperacidophilic bacterium, that has been determined in an apo-form, in complex with its natural ligand (acetyl coenzyme A), and in complex with a product of reaction (coenzyme A) obtained by cocrystallization with spermidine. Sequence and structural analysis reveals that Ta0374 belongs to a novel protein family, PaiA, involved in the negative control of sporulation and degradative enzyme production. The crystal structure of Ta0374 confirms that it binds acetyl coenzyme A in a way similar to other GNATs and is capable of acetylating spermidine. Based on structural and docking analysis, it is expected that Glu53 and Tyr93 are key residues for recognizing spermidine. Additionally, we find that the purification His-Tag in the apo-form structure of Ta0374 prevents binding of acetyl coenzyme A in the crystal, though not in solution, and affects a chain-flip rotation of "motif A" which is the most conserved sequence among canonical acetyltransferases. Proteins 2011; (c) 2011 Wiley-Liss, Inc.
Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production.,Filippova EV, Shuvalova L, Minasov G, Kiryukhina O, Zhang Y, Clancy S, Radhakrishnan I, Joachimiak A, Anderson WF Proteins. 2011 Aug;79(8):2566-77. doi: 10.1002/prot.23062. Epub 2011 Jun, 1. PMID:21633970[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Filippova EV, Shuvalova L, Minasov G, Kiryukhina O, Zhang Y, Clancy S, Radhakrishnan I, Joachimiak A, Anderson WF. Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production. Proteins. 2011 Aug;79(8):2566-77. doi: 10.1002/prot.23062. Epub 2011 Jun, 1. PMID:21633970 doi:10.1002/prot.23062
- ↑ Kuhn ML, Majorek KA, Minor W, Anderson WF. Broad-substrate screen as a tool to identify substrates for bacterial Gcn5-related N-acetyltransferases with unknown substrate specificity. Protein Sci. 2013 Feb;22(2):222-30. doi: 10.1002/pro.2199. Epub 2012 Dec 17. PMID:23184347 doi:http://dx.doi.org/10.1002/pro.2199
- ↑ Filippova EV, Shuvalova L, Minasov G, Kiryukhina O, Zhang Y, Clancy S, Radhakrishnan I, Joachimiak A, Anderson WF. Crystal structure of the novel PaiA N-acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production. Proteins. 2011 Aug;79(8):2566-77. doi: 10.1002/prot.23062. Epub 2011 Jun, 1. PMID:21633970 doi:10.1002/prot.23062
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