4NJE

Crystal structure of Pyrococcus furiosus L-asparaginase with ligand

4NJE の概要

• エントリーDOI: 10.2210/pdb4nje/pdb
• 分子名称: L-asparaginase, ASPARTIC ACID, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Pyrococcus furiosus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38474.30

構造登録者

Sharma, P.,Tomar, R.,Singh, S.,Yadav, S.P.S.,Ashish,Kundu, B. (登録日: 2013-11-09, 公開日: 2014-12-10, 最終更新日: 2024-11-20)

主引用文献

Tomar, R.,Sharma, P.,Srivastava, A.,Bansal, S.,Kundu, B.
Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains.
Acta Crystallogr.,Sect.D, 70:3187-3197, 2014

PubMed Abstract: Covalent linkers bridging the domains of multidomain proteins are considered to be crucial for assembly and function. In this report, an exception in which the linker of a two-domain dimeric L-asparaginase from Pyrococcus furiosus (PfA) was found to be dispensable is presented. Domains of this enzyme assembled without the linker into a conjoined tetrameric form that exhibited higher activity than the parent enzyme. The global shape and quaternary structure of the conjoined PfA were also similar to the wild-type PfA, as observed by their solution scattering profiles and X-ray crystallographic data. Comparison of the crystal structures of substrate-bound and unbound enzymes revealed an altogether new active-site composition and mechanism of action. Thus, conjoined PfA is presented as a unique enzyme obtained through noncovalent, linker-less assembly of constituent domains that is stable enough to function efficiently at elevated temperatures.

PubMed: 25478837
DOI: 10.1107/S1399004714023414

実験手法

X-RAY DIFFRACTION (2.5 Å)