1tiq

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{{Seed}}
 
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[[Image:1tiq.png|left|200px]]
 
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==Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.==
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The line below this paragraph, containing "STRUCTURE_1tiq", creates the "Structure Box" on the page.
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<StructureSection load='1tiq' size='340' side='right'caption='[[1tiq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<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>
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{{STRUCTURE_1tiq| PDB=1tiq | SCENE= }}
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ti/1tiq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tiq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.===
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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<ref>PMID:16210326</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16210326}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1tiq" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16210326 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16210326}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1TIQ is a 2 chains structure of sequences from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16210326 16210326]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Acton, T B.]]
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[[Category: Large Structures]]
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[[Category: Forouhar, F.]]
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[[Category: Acton TB]]
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[[Category: Hunt, J F.]]
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[[Category: Forouhar F]]
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[[Category: Lee, I.]]
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[[Category: Hunt JF]]
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[[Category: Montelione, G T.]]
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[[Category: Lee I]]
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[[Category: NESG, Northeast Structural Genomics Consortium.]]
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[[Category: Montelione GT]]
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[[Category: Shen, J.]]
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[[Category: Shen J]]
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[[Category: Tong, L.]]
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[[Category: Tong L]]
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[[Category: Vorobiev, S M.]]
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[[Category: Vorobiev SM]]
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[[Category: Xiao, R.]]
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[[Category: Xiao R]]
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[[Category: Alpha-beta protein]]
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[[Category: Nesg]]
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[[Category: Northeast structural genomics consortium]]
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[[Category: Protein structure initiative]]
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[[Category: Psi]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Nov 16 16:11:39 2008''
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Current revision

Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.

PDB ID 1tiq

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