4RA9: Crystal Structure Of Conjoint Pyrococcus Furiosus L-asparaginase With Citrate

Citation:
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.
PDB ID: 4RA9Download
MMDB ID: 125443
PDB Deposition Date: 2014/9/9
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 2.05  Å
Source Organism:
Similar Structures:
Biological Unit for 4RA9: dimeric; determined by author and by software (PISA)
Molecular Components in 4RA9
Label Count Molecule
Proteins (2 molecules)
1
L-asparaginase
Molecule annotation
1
L-asparaginase
Molecule annotation
Chemicals (8 molecules)
1
2
2
4
3
2
* Click molecule labels to explore molecular sequence information.

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