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Sortase A
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Sortase A : ウィキペディア英語版
Sortase A

Sortase A (, ''SrtA'', ''SrtA protein'', ''SrtA sortase'') is an enzyme. This enzyme catalyses the following chemical reaction
: The enzyme catalyses a cell wall sorting reaction, in which a surface protein with a sorting signal containing a LPXTG motif, is cleaved between the Thr and Gly residue.
This enzyme belongs to the peptidase family C60.
==Structure of Sortase A==
Sortase A has an eight stranded β-barrel fold with a hydrophobic cleft formed by β7-β8 strands. This cleft is surrounded by β3-β4, β2-β3, β6-β7, and β7-β8 loops. The catalytic cysteine residue is found in this cleft and accepts subsequent binding of a nucleophilic agent. The β3-β4 loop contains a calcium binding site which binds calcium via coordination to a residue in the β6-β7 loop. Such binding slows down the motion of the β6-β7 loop, allowing the substrate of Sortase to bind and increase its activity eightfold.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
ウィキペディアで「Sortase A」の詳細全文を読む



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