Volume 241, No. 3

Baier, Kerstin; Nicklisch, Sabine; Maldener, Iris; Lockau, Wolfgang

doi:10.1111/j.1432-1033.1997.00214.x

Cited by 4 publications

(4 citation statements)

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“…24 It was suggested that the prodomain might help overcome energy barriers to a productive folding pathway. Other examples of prodomain mediated folding have been found in all four mechanistic families of proteases: serine proteases, [25][26][27][28][29][30] aspartic proteases, [31][32][33] metalloproteases, [34][35][36][37][38] and cysteine proteases. 39…”

Section: Identification Of Prosequencesmentioning

confidence: 99%

Prodomains and Protein Folding Catalysis

Bryan

2002

Chem. Rev.

107

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Section: Identification Of Prosequencesmentioning

confidence: 99%

Prodomains and Protein Folding Catalysis

Bryan

2002

Chem. Rev.

107

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“…The mature domains alone are not folded into an active form but are folded into an inactive form with a molten globular-like structure in the absence of propeptides (Eder et al, 1993;Shinde & Inouye, 1995). Requirement of a propeptide for the maturation of its cognate mature domain has also been reported not only for other members of the subtilase family (Baier et al, 1996;Marie-Claire et al, 2001;Basak & Lazure, 2003), but also for other proteases (Silen & Agard, 1989;Smith & Gottesman, 1989;Winther & Sorensen, 1991;O'Donohue & Beaumont, 1996;Marie-Claire et al, 1999;Nirasawa et al, 1999).…”

Section: Introductionmentioning

confidence: 96%

Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon

et al. 2006

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Crystallization of and preliminary crystallographic studies on an active-site mutant of pro-Tk-subtilisin from the hyperthermophilic archaeon Thermococcus kodakaraensis were performed. The crystal was grown at 277 K by the sitting-drop vapour-diffusion method. Native X-ray diffraction data were collected to 2.3 Å resolution using synchrotron radiation from station BL41XU at SPring-8. The crystal belongs to the orthorhombic space group I222, with unitcell parameters a = 92.69, b = 121.78, c = 77.53 Å . Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient V M was calculated to be 2.6 Å 3 Da À1 and the solvent content was 53.1%.

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“…The mature domains alone are not an active form but an inactive form with a molten globule-like structure in the absence of propeptides (7,10). Dependence on the propeptide for maturation of its cognate mature domain has been reported not only for other members of the subtilase family (11)(12)(13) but also for other proteases (14 -19).…”

mentioning

confidence: 99%

Crystal Structure of Unautoprocessed Precursor of Subtilisin from a Hyperthermophilic Archaeon

Tanaka¹,

Saito²,

Chon³

et al. 2007

Journal of Biological Chemistry

132

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The crystal structure of an active site mutant of pro-Tk-subtilisin (pro-S324A) from the hyperthermophilic archaeon Thermococcus kodakaraensis was determined at 2.3 Å resolution. The overall structure of this protein is similar to those of bacterial subtilisin-propeptide complexes, except that the peptide bond linking the propeptide and mature domain contacts with the active site, and the mature domain contains six Ca 2؉ binding sites. The Ca-1 site is conserved in bacterial subtilisins but is formed prior to autoprocessing, unlike the corresponding sites of bacterial subtilisins. All other Ca 2؉ -binding sites are unique in the pro-S324A structure and are located at the surface loops. Four of them apparently contribute to the stability of the central ␣␤␣ substructure of the mature domain. The CD spectra, 1-anilino-8-naphthalenesulfonic acid fluorescence spectra, and sensitivities to chymotryptic digestion of this protein indicate that the conformation of pro-S324A is changed from an unstable molten globule-like structure to a stable native one upon Ca 2؉ binding. Another active site mutant, pro-S324C, was shown to be autoprocessed to form a propeptide-mature domain complex in the presence of Ca 2؉ . The CD spectra of this protein indicate that the structure of pro-S324C is changed upon Ca 2؉ binding like pro-S324A but is not seriously changed upon subsequent autoprocessing. These results suggest that the maturation process of Tk-subtilisin is different from that of bacterial subtilisins in terms of the requirement of Ca 2؉ for folding of the mature domain and completion of the folding process prior to autoprocessing.

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Volume 241, No. 3

Cited by 4 publications

References 0 publications

Prodomains and Protein Folding Catalysis

Prodomains and Protein Folding Catalysis

Crystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeon

Crystal Structure of Unautoprocessed Precursor of Subtilisin from a Hyperthermophilic Archaeon

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