1tiq
From Proteopedia
(New page: 200px<br /><applet load="1tiq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tiq, resolution 1.9Å" /> '''Crystal Structure of ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1tiq.gif|left|200px]]<br /><applet load="1tiq" size=" | + | [[Image:1tiq.gif|left|200px]]<br /><applet load="1tiq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tiq, resolution 1.9Å" /> | caption="1tiq, resolution 1.9Å" /> | ||
'''Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.'''<br /> | '''Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacillus subtilis PaiA has been implicated in the negative control of | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TIQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4, COA and DTT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1TIQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=DTT:'>DTT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TIQ OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Acton, T | + | [[Category: Acton, T B.]] |
[[Category: Forouhar, F.]] | [[Category: Forouhar, F.]] | ||
| - | [[Category: Hunt, J | + | [[Category: Hunt, J F.]] |
[[Category: Lee, I.]] | [[Category: Lee, I.]] | ||
| - | [[Category: Montelione, G | + | [[Category: Montelione, G T.]] |
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: Shen, J.]] | [[Category: Shen, J.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
| - | [[Category: Vorobiev, S | + | [[Category: Vorobiev, S M.]] |
[[Category: Xiao, R.]] | [[Category: Xiao, R.]] | ||
[[Category: COA]] | [[Category: COA]] | ||
| Line 33: | Line 33: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:55 2008'' |
Revision as of 13:13, 21 February 2008
|
Crystal Structure of an Acetyltransferase (PaiA) in complex with CoA and DTT from Bacillus subtilis, Northeast Structural Genomics Target SR64.
Overview
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.
About this Structure
1TIQ is a Single protein structure of sequence from Bacillus subtilis with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:13:55 2008
Categories: Bacillus subtilis | Single protein | Acton, T B. | Forouhar, F. | Hunt, J F. | Lee, I. | Montelione, G T. | NESG, Northeast Structural Genomics Consortium. | Shen, J. | Tong, L. | Vorobiev, S M. | Xiao, R. | COA | DTT | SO4 | Alpha-beta protein | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi | Structural genomics
