4q0m
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0m OCA], [http://pdbe.org/4q0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q0m RCSB], [http://www.ebi.ac.uk/pdbsum/4q0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0m ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0m OCA], [http://pdbe.org/4q0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q0m RCSB], [http://www.ebi.ac.uk/pdbsum/4q0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:25478837</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4q0m" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Asparaginase 3D structures|Asparaginase 3D structures]] | *[[Asparaginase 3D structures|Asparaginase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:41, 1 January 2020
Crystal structure of Pyrococcus furiosus L-asparaginase
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Categories: Asparaginase | Large Structures | Pyrfu | Ashish | Kundu, B | Sharma, P | Singh, S | Tomar, R | Yadav, S P.S | Hydrolase
