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| | ==Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.== | | ==Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.== |
| - | <StructureSection load='1tiq' size='340' side='right' caption='[[1tiq]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='1tiq' size='340' side='right'caption='[[1tiq]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tiq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TIQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tiq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TIQ 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>, <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9Å</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=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAIA, BSU32150 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=1tiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tiq OCA], [https://pdbe.org/1tiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tiq RCSB], [https://www.ebi.ac.uk/pdbsum/1tiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tiq ProSAT], [https://www.topsan.org/Proteins/NESGC/1tiq TOPSAN]</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=1tiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tiq OCA], [http://pdbe.org/1tiq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tiq RCSB], [http://www.ebi.ac.uk/pdbsum/1tiq PDBsum], [http://www.topsan.org/Proteins/NESGC/1tiq TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAIA_BACSU PAIA_BACSU]] Possesses N1-acetyltransferase activity toward polyamine substrates including spermidine and spermine. Can acetylate both spermidine and spermine. In this way it may function in regulating intracellular polyamine concentrations and/or binding capabilities. In addition to preventing toxicity due to polyamine excess, this function may also serve to regulate expression of certain bacterial gene products such as those involved in sporulation.<ref>PMID:16210326</ref> | + | [https://www.uniprot.org/uniprot/PAIA_BACSU PAIA_BACSU] Possesses N1-acetyltransferase activity toward polyamine substrates including spermidine and spermine. Can acetylate both spermidine and spermine. In this way it may function in regulating intracellular polyamine concentrations and/or binding capabilities. In addition to preventing toxicity due to polyamine excess, this function may also serve to regulate expression of certain bacterial gene products such as those involved in sporulation.<ref>PMID:16210326</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/ti/1tiq_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ti/1tiq_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: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Acton, T B]] | + | [[Category: Large Structures]] |
| - | [[Category: Forouhar, F]] | + | [[Category: Acton TB]] |
| - | [[Category: Hunt, J F]] | + | [[Category: Forouhar F]] |
| - | [[Category: Lee, I]] | + | [[Category: Hunt JF]] |
| - | [[Category: Montelione, G T]] | + | [[Category: Lee I]] |
| - | [[Category: Structural genomic]] | + | [[Category: Montelione GT]] |
| - | [[Category: Shen, J]] | + | [[Category: Shen J]] |
| - | [[Category: Tong, L]] | + | [[Category: Tong L]] |
| - | [[Category: Vorobiev, S M]] | + | [[Category: Vorobiev SM]] |
| - | [[Category: Xiao, R]] | + | [[Category: Xiao R]] |
| - | [[Category: Alpha-beta protein]]
| + | |
| - | [[Category: Nesg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
1tiq is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.9Å |
| Ligands: | , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN |
Function
PAIA_BACSU Possesses N1-acetyltransferase activity toward polyamine substrates including spermidine and spermine. Can acetylate both spermidine and spermine. In this way it may function in regulating intracellular polyamine concentrations and/or binding capabilities. In addition to preventing toxicity due to polyamine excess, this function may also serve to regulate expression of certain bacterial gene products such as those involved in sporulation.[1]
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
Bacillus subtilis PaiA has been implicated in the negative control of sporulation as well as production of degradative enzymes. PaiA shares recognizable sequence homology with N-acetyltransferases, including those that can acetylate spermidine/spermine substrates. We have determined the crystal structure of PaiA in complex with CoA at 1.9 A resolution and found that PaiA is a member of the N-acetyltransferase superfamily of enzymes. Unexpectedly, we observed the binding of an oxidized CoA dimer in the active site of PaiA, and the structural information suggests the substrates of the enzyme could be linear, positively charged compounds. Our biochemical characterization is also consistent with this possibility, since purified PaiA possesses N1-acetyltransferase activity toward polyamine substrates including spermidine and spermine. Further, conditional overexpression of PaiA in bacteria results in increased acetylation of endogenous spermidine pools. Thus, our structural and biochemical analyses indicate that PaiA is a novel N-acetyltransferase capable of acetylating both spermidine and spermine. In this way, the pai operon may function in regulating intracellular polyamine concentrations and/or binding capabilities. In addition to preventing toxicity due to polyamine excess, this function may also serve to regulate expression of certain bacterial gene products such as those involved in sporulation.
Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase.,Forouhar F, Lee IS, Vujcic J, Vujcic S, Shen J, Vorobiev SM, Xiao R, Acton TB, Montelione GT, Porter CW, Tong L J Biol Chem. 2005 Dec 2;280(48):40328-36. Epub 2005 Oct 6. PMID:16210326[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Forouhar F, Lee IS, Vujcic J, Vujcic S, Shen J, Vorobiev SM, Xiao R, Acton TB, Montelione GT, Porter CW, Tong L. Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase. J Biol Chem. 2005 Dec 2;280(48):40328-36. Epub 2005 Oct 6. PMID:16210326 doi:10.1074/jbc.M505332200
- ↑ Forouhar F, Lee IS, Vujcic J, Vujcic S, Shen J, Vorobiev SM, Xiao R, Acton TB, Montelione GT, Porter CW, Tong L. Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase. J Biol Chem. 2005 Dec 2;280(48):40328-36. Epub 2005 Oct 6. PMID:16210326 doi:10.1074/jbc.M505332200
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