About: Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity

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About: Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity
Creator	Tang, Bo Lai, Luhua Li, Chunmei Ma, Xiaomin Qi, Yifei Shi, Hailing Teng, Xin
Source	Medline; PMC
abstract	The SARS 3C-like proteinase (SARS-3CLpro), which is the main proteinase of the SARS coronavirus, is essential to the virus life cycle. This enzyme has been shown to be active as a dimer in which only one protomer is active. However, it remains unknown how the dimer structure maintains an active monomer conformation. It has been observed that the Ser139-Leu141 loop forms a short 3(10)-helix that disrupts the catalytic machinery in the inactive monomer structure. We have tried to disrupt this helical conformation by mutating L141 to T in the stable inactive monomer G11A/R298A/Q299A. The resulting tetra-mutant G11A/L141T/R298A/Q299A is indeed enzymatically active as a monomer. Molecular dynamics simulations revealed that the L141T mutation disrupts the 3(10)-helix and helps to stabilize the active conformation. The coil-3(10)-helix conformational transition of the Ser139-Leu141 loop serves as an enzyme activity switch. Our study therefore indicates that the dimer structure can stabilize the active conformation but is not a required structure in the evolution of the active enzyme, which can also arise through simple mutations.
has issue date	2016-02-16(xsd:dateTime)
bibo:doi	10.1038/srep20918
bibo:pmid	26879383
has license	cc-by
sha1sum (hex)	5f7b5b1f4748ede29130df5606fd51f4820edc20
schema:url	https://doi.org/10.1038/srep20918
resource representing a document's title	Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity
has PubMed Central identifier	PMC4754693
has PubMed identifier	26879383
schema:publication	Sci Rep
resource representing a document's body	covid:5f7b5b1f4748ede29130df5606fd51f4820edc20#body_text
is schema:about of	named entity 'mutation' named entity 'conformation' named entity 'enzyme' named entity 'observed' named entity 'Flexibility' covid:arg/5f7b5b1f4748ede29130df5606fd51f4820edc20 named entity 'monomer' named entity 'conformation' named entity 'enzymatically active' named entity 'dimer' named entity 'study' named entity 'evolution' named entity 'proteinase' named entity 'helix' named entity 'Molecular dynamics' named entity 'dimer' named entity 'helix' named entity 'dimer' named entity 'enzyme' named entity 'proteinase' named entity 'monomer' named entity 'SARS' named entity 'SARS' named entity '3CLpro' named entity 'transition' named entity 'life cycle' named entity 'enzyme' named entity 'enzyme activity' named entity 'enzyme' named entity 'dimer' named entity 'point charge' named entity 'monomer' named entity 'Monomer' named entity 'dimerization' named entity 'coronaviruses' named entity 'dimer' named entity 'protomer' named entity 'mutation' named entity 'carbonic anhydrase' named entity 'enzyme' named entity 'substrate binding site' named entity 'catalytic site' named entity 'substrate' named entity 'helix' named entity '21h' named entity 'monomer' named entity 'monomer' named entity 'solvate' named entity 'oxyanion hole' named entity 'enzyme' named entity 'PDB' named entity 'proteinase' named entity 'active site' named entity 'LINear' named entity 'dimer' named entity 'SARS' named entity 'enzyme' named entity 'wild-type' named entity 'ovalbumin' named entity 'substrate' named entity 'substrate' named entity 'Gln' named entity 'enzyme' named entity 'binding site' named entity 'PDB' named entity 'helix' named entity 'Gromacs' named entity 'La Jolla' named entity 'monomer' named entity 'Thr' named entity 'ND1' named entity 'protomer' named entity 'helix' named entity 'protease' named entity 'Thr'

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