4RA6
Crystal structure of linker less Pyrococcus furiosus L-asparaginase
Summary for 4RA6
| Entry DOI | 10.2210/pdb4ra6/pdb |
| Related | 4RA9 |
| Descriptor | L-asparaginase, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Pyrococcus furiosus DSM 3638 More |
| Total number of polymer chains | 4 |
| Total formula weight | 76958.67 |
| Authors | Sharma, P.,Tomar, R.,Ashish,Kundu, B. (deposition date: 2014-09-09, release date: 2014-12-10, Last modification date: 2024-11-06) |
| 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 Cited by 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: 25478837DOI: 10.1107/S1399004714023414 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.503 Å) |
Structure validation
Download full validation report
