4nje

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Crystal structure of Pyrococcus furiosus L-asparaginase with ligand

Structural highlights

4nje is a 2 chain structure with sequence from Pyrococcus furiosus DSM 3638. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:ASP
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASPG_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 PubMed

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.

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.

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See Also

References

  1. ↑ Bansal S, Gnaneswari D, Mishra P, Kundu B. Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus. Biochemistry (Mosc). 2010 Mar;75(3):375-81. doi: 10.1134/s0006297910030144. PMID:20370616 doi:http://dx.doi.org/10.1134/s0006297910030144
  2. ↑ Bansal S, Srivastava A, Mukherjee G, Pandey R, Verma AK, Mishra P, Kundu B. Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action. FASEB J. 2012 Mar;26(3):1161-71. doi: 10.1096/fj.11-191254. Epub 2011 Dec 13. PMID:22166247 doi:http://dx.doi.org/10.1096/fj.11-191254
  3. ↑ 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 D Biol Crystallogr. 2014 Dec 1;70(Pt 12):3187-97. doi:, 10.1107/S1399004714023414. Epub 2014 Nov 22. PMID:25478837 doi:http://dx.doi.org/10.1107/S1399004714023414

Contents


PDB ID 4nje

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