SrasV1, PubMed, Corpus, bibRecord, 002343

The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain.

Identifieur interne : 002343 ( PubMed/Corpus ); précédent : 002342; suivant : 002344

The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain.

Auteurs : Jiahai Shi ; Jianxing Song

Source :

The FEBS journal [ 1742-464X ] ; 2006.

RBID : pubmed:16478476

English descriptors

KwdEn :
- Catalysis, Catalytic Domain, Circular Dichroism, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Dimerization, Light, Models, Molecular, Mutagenesis, Site-Directed, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (enzymology), SARS Virus (genetics), Scattering, Radiation, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
MESH :
- chemical , chemistry : Cysteine Endopeptidases, Recombinant Fusion Proteins, Viral Proteins.
- chemical , genetics : Cysteine Endopeptidases, Recombinant Fusion Proteins, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Recombinant Fusion Proteins, Viral Proteins.
- enzymology : SARS Virus.
- genetics : SARS Virus.
- Catalysis, Catalytic Domain, Circular Dichroism, Dimerization, Light, Models, Molecular, Mutagenesis, Site-Directed, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Scattering, Radiation.

Abstract

The 3C-like protease of the severe acute respiratory syndrome (SARS) coronavirus has a C-terminal extra domain in addition to the chymotrypsin-fold adopted by picornavirus 3C proteases hosting the complete catalytic machinery. Previously we identified the extra domain to be involved in enzyme dimerization which has been considered essential for the catalytic activity. In an initial attempt to map out the extra-domain residues critical for dimerization, we have systematically generated 15 point mutations, five deletions and one triple mutation and subsequently characterized them by enzymatic assay, dynamic light scattering, CD and NMR spectroscopy. The results led to identification of four regions critical for enzyme dimerization. Interestingly, Asn214Ala mutant with a significant tendency to form a monomer still retained approximately 30% activity, indicating that the relationship between the activity and dimerization might be very complex. Very surprisingly, two regions (one over Ser284-Thr285-Ile286 and another around Phe291) were discovered on which Ala-mutations significantly increased the enzymatic activities. Based on this, a super-active triple-mutant STI/A with a 3.7-fold activity enhancement was thus engineered by mutating residues Ser284, Thr285 and Ile286 to Ala. The dynamic light scattering, CD and NMR characterizations indicate that the wild-type (WT) and STI/A mutant share similar structural and dimerization properties, thus implying that in addition to dimerization, the extra domain might have other mechanisms to regulate the catalytic machinery. We rationalized these results based on the enzyme structure and consequently observed an interesting picture: the majority of the dimerization-critical residues plus Ser284-Thr285-Ile286 and Phe291 are clustered together to form a nano-scale channel passing through the central region of the enzyme. We therefore speculate that this channel might play a role in relaying regulatory effects from the extra domain to the catalytic machinery.

DOI: 10.1111/j.1742-4658.2006.05130.x
PubMed: 16478476

Links to Exploration step

pubmed:16478476

Le document en format XML

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<term>Cysteine Endopeptidases (genetics)</term>
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<term>Mutagenesis, Site-Directed</term>
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<front><div type="abstract" xml:lang="en">The 3C-like protease of the severe acute respiratory syndrome (SARS) coronavirus has a C-terminal extra domain in addition to the chymotrypsin-fold adopted by picornavirus 3C proteases hosting the complete catalytic machinery. Previously we identified the extra domain to be involved in enzyme dimerization which has been considered essential for the catalytic activity. In an initial attempt to map out the extra-domain residues critical for dimerization, we have systematically generated 15 point mutations, five deletions and one triple mutation and subsequently characterized them by enzymatic assay, dynamic light scattering, CD and NMR spectroscopy. The results led to identification of four regions critical for enzyme dimerization. Interestingly, Asn214Ala mutant with a significant tendency to form a monomer still retained approximately 30% activity, indicating that the relationship between the activity and dimerization might be very complex. Very surprisingly, two regions (one over Ser284-Thr285-Ile286 and another around Phe291) were discovered on which Ala-mutations significantly increased the enzymatic activities. Based on this, a super-active triple-mutant STI/A with a 3.7-fold activity enhancement was thus engineered by mutating residues Ser284, Thr285 and Ile286 to Ala. The dynamic light scattering, CD and NMR characterizations indicate that the wild-type (WT) and STI/A mutant share similar structural and dimerization properties, thus implying that in addition to dimerization, the extra domain might have other mechanisms to regulate the catalytic machinery. We rationalized these results based on the enzyme structure and consequently observed an interesting picture: the majority of the dimerization-critical residues plus Ser284-Thr285-Ile286 and Phe291 are clustered together to form a nano-scale channel passing through the central region of the enzyme. We therefore speculate that this channel might play a role in relaying regulatory effects from the extra domain to the catalytic machinery.</div>
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<Abstract><AbstractText>The 3C-like protease of the severe acute respiratory syndrome (SARS) coronavirus has a C-terminal extra domain in addition to the chymotrypsin-fold adopted by picornavirus 3C proteases hosting the complete catalytic machinery. Previously we identified the extra domain to be involved in enzyme dimerization which has been considered essential for the catalytic activity. In an initial attempt to map out the extra-domain residues critical for dimerization, we have systematically generated 15 point mutations, five deletions and one triple mutation and subsequently characterized them by enzymatic assay, dynamic light scattering, CD and NMR spectroscopy. The results led to identification of four regions critical for enzyme dimerization. Interestingly, Asn214Ala mutant with a significant tendency to form a monomer still retained approximately 30% activity, indicating that the relationship between the activity and dimerization might be very complex. Very surprisingly, two regions (one over Ser284-Thr285-Ile286 and another around Phe291) were discovered on which Ala-mutations significantly increased the enzymatic activities. Based on this, a super-active triple-mutant STI/A with a 3.7-fold activity enhancement was thus engineered by mutating residues Ser284, Thr285 and Ile286 to Ala. The dynamic light scattering, CD and NMR characterizations indicate that the wild-type (WT) and STI/A mutant share similar structural and dimerization properties, thus implying that in addition to dimerization, the extra domain might have other mechanisms to regulate the catalytic machinery. We rationalized these results based on the enzyme structure and consequently observed an interesting picture: the majority of the dimerization-critical residues plus Ser284-Thr285-Ile286 and Phe291 are clustered together to form a nano-scale channel passing through the central region of the enzyme. We therefore speculate that this channel might play a role in relaying regulatory effects from the extra domain to the catalytic machinery.</AbstractText>
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</pubmed>
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Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Corpus

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002343 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 002343 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    PubMed
   |étape=   Corpus
   |type=    RBID
   |clé=     pubmed:16478476
   |texte=   The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i   -Sk "pubmed:16478476" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

This area was generated with Dilib version V0.6.33.
Data generation: Tue Apr 28 14:49:16 2020. Site generation: Sat Mar 27 22:06:49 2021

	Serveur d'exploration SRAS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration SRAS

The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain.

The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki