4NJE

Crystal structure of Pyrococcus furiosus L-asparaginase with ligand

Summary for 4NJE

• Entry DOI: 10.2210/pdb4nje/pdb
• Descriptor: L-asparaginase, ASPARTIC ACID, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 2
• Total formula weight: 38474.30

Authors

Sharma, P.,Tomar, R.,Singh, S.,Yadav, S.P.S.,Ashish,Kundu, B. (deposition date: 2013-11-09, release date: 2014-12-10, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)