5CMT

Fic protein from Neisseria meningitidis (NmFic) mutant E156R Y183F in dimeric form

5CMT の概要

• エントリーDOI: 10.2210/pdb5cmt/pdb
• 分子名称: Adenosine monophosphate-protein transferase NmFic, GLYCEROL, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: fic protein, amp-transferase, dimer, transferase
• 由来する生物種: Neisseria meningitidis serogroup B
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22425.78

構造登録者

Stanger, F.V.,Schirmer, T. (登録日: 2015-07-17, 公開日: 2016-01-27, 最終更新日: 2024-01-10)

主引用文献

Stanger, F.V.,Burmann, B.M.,Harms, A.,Aragao, H.,Mazur, A.,Sharpe, T.,Dehio, C.,Hiller, S.,Schirmer, T.
Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification.
Proc.Natl.Acad.Sci.USA, 113:E529-E537, 2016

PubMed Abstract: Filamentation induced by cyclic AMP (FIC)-domain enzymes catalyze adenylylation or other posttranslational modifications of target proteins to control their function. Recently, we have shown that Fic enzymes are autoinhibited by an α-helix (αinh) that partly obstructs the active site. For the single-domain class III Fic proteins, the αinh is located at the C terminus and its deletion relieves autoinhibition. However, it has remained unclear how activation occurs naturally. Here, we show by structural, biophysical, and enzymatic analyses combined with in vivo data that the class III Fic protein NmFic from Neisseria meningitidis gets autoadenylylated in cis, thereby autonomously relieving autoinhibition and thus allowing subsequent adenylylation of its target, the DNA gyrase subunit GyrB. Furthermore, we show that NmFic activation is antagonized by tetramerization. The combination of autoadenylylation and tetramerization results in nonmonotonic concentration dependence of NmFic activity and a pronounced lag phase in the progress of target adenylylation. Bioinformatic analyses indicate that this elaborate dual-control mechanism is conserved throughout class III Fic proteins.

PubMed: 26787847
DOI: 10.1073/pnas.1516930113

実験手法

X-RAY DIFFRACTION (0.99 Å)