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Crystal structure of Pyrococcus furiosus L-asparaginase with ligand
Structural highlights
FunctionASPG_PYRFU Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Displays no glutaminase activity, a highly desirable therapeutic property.[1] [2] Publication Abstract from PubMedCovalent 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. Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains.,Tomar R, Sharma P, Srivastava A, Bansal S, Kundu B Acta Crystallogr D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3187-97. doi:, 10.1107/S1399004714023414. Epub 2014 Nov 22. PMID:25478837[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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