1TIQ

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

1TIQ の概要

• エントリーDOI: 10.2210/pdb1tiq/pdb
• 分子名称: Protease synthase and sporulation negative regulatory protein PAI 1, COENZYME A, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (5 entities in total)
• 機能のキーワード: alpha-beta protein, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, transcription
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45583.41

構造登録者

Forouhar, F.,Lee, I.,Shen, J.,Vorobiev, S.M.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Hunt, J.F.,Tong, L.,Northeast Structural Genomics Consortium (NESG) (登録日: 2004-06-02, 公開日: 2004-07-13, 最終更新日: 2024-10-30)

主引用文献

Forouhar, F.,Lee, I.S.,Vujcic, J.,Vujcic, S.,Shen, J.,Vorobiev, S.M.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Porter, C.W.,Tong, L.
Structural and functional evidence for Bacillus subtilis PaiA as a novel N1-spermidine/spermine acetyltransferase.
J.Biol.Chem., 280:40328-40336, 2005

PubMed Abstract: 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.

PubMed: 16210326
DOI: 10.1074/jbc.M505332200

実験手法

X-RAY DIFFRACTION (1.9 Å)