Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
02 06 2021
02 06 2021
Historique:
received:
16
12
2020
accepted:
13
05
2021
entrez:
3
6
2021
pubmed:
4
6
2021
medline:
9
11
2021
Statut:
epublish
Résumé
Salt-bridges play a key role in the thermostability of proteins adapted in stress environments whose intrinsic basis remains to be understood. We find that the higher hydrophilicity of PfP than that of HuP is due to the charged but not the polar residues. The primary role of these residues is to enhance the salt-bridges and their ME. Unlike HuP, PfP has made many changes in its intrinsic property to strengthen the salt-bridge. First, the desolvation energy is reduced by directing the salt-bridge towards the surface. Second, it has made bridge-energy more favorable by recruiting energetically advantageous partners with high helix-propensity among the six possible salt-bridge pairs. Third, ME-residues that perform intricate interactions have increased their energy contribution by making major changes in their binary properties. The use of salt-bridge partners as ME-residues, and ME-residues' overlapping usage, predominant in helices, and energetically favorable substitution are some of the favorable features of PfP compared to HuP. These changes in PfP reduce the unfavorable, increase the favorable ME-energy. Thus, the per salt-bridge stability of PfP is greater than that of HuP. Further, unfavorable target ME-residues can be identified whose mutation can increase the stability of salt-bridge. The study applies to other similar systems.
Identifiants
pubmed: 34078944
doi: 10.1038/s41598-021-90723-4
pii: 10.1038/s41598-021-90723-4
pmc: PMC8172842
doi:
Substances chimiques
Prolyl Oligopeptidases
EC 3.4.21.26
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
11553Références
Bioinformation. 2019 Mar 15;15(3):214-225
pubmed: 31354198
Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W665-7
pubmed: 15215472
Biophys J. 1992 Dec;63(6):1483-6
pubmed: 1489908
Nature. 1989 May 4;339(6219):31-6
pubmed: 2524006
Proc Natl Acad Sci U S A. 2001 Aug 28;98(18):10037-41
pubmed: 11517324
Protein Eng. 2000 Mar;13(3):179-91
pubmed: 10775659
Protein Eng. 1996 Mar;9(3):265-71
pubmed: 8736493
Bioinformation. 2020 Nov 30;16(11):900-909
pubmed: 34803266
Science. 1978 Sep 29;201(4362):1187-91
pubmed: 694508
Biochemistry. 1990 Aug 7;29(31):7133-55
pubmed: 2207096
Biochemistry. 1991 Jul 23;30(29):7142-53
pubmed: 1854726
Protein Sci. 2005 May;14(5):1293-304
pubmed: 15802649
Bioinformation. 2019 Feb 3;15(1):61-67
pubmed: 31360001
Eur J Biochem. 1998 Jul 15;255(2):336-46
pubmed: 9716374
J Mol Biol. 2000 Sep 8;302(1):205-17
pubmed: 10964570
Biophys J. 2016 Jun 7;110(11):2328-2341
pubmed: 27276251
Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12742-7
pubmed: 16120678
Nature. 1975 May 15;255(5505):256-9
pubmed: 1143325
Proc Natl Acad Sci U S A. 1981 Jun;78(6):3824-8
pubmed: 6167991
FEBS Lett. 1997 Nov 24;418(1-2):43-6
pubmed: 9414092
Bioinformation. 2018 Dec 22;14(9):525-529
pubmed: 31435151
FEMS Microbiol Rev. 1996 May;18(2-3):105-17
pubmed: 8639325
Protein Sci. 1994 Feb;3(2):211-26
pubmed: 8003958
Biochemistry. 1990 Aug 21;29(33):7584-92
pubmed: 2271518
J Mol Biol. 1999 Nov 12;293(5):1241-55
pubmed: 10547298
Proteins. 1997 Nov;29(3):309-20
pubmed: 9365986
J Biotechnol. 2000 May 26;79(3):193-203
pubmed: 10867180
Nature. 1986 Sep 25-Oct 1;323(6086):356-8
pubmed: 3020429
Science. 1973 Jul 20;181(4096):223-30
pubmed: 4124164
J Mol Recognit. 2004 Jan-Feb;17(1):1-16
pubmed: 14872533
Nature. 1988 Dec 15;336(6200):651-6
pubmed: 3200317
Microbiol Mol Biol Rev. 2001 Mar;65(1):1-43
pubmed: 11238984
Methods Enzymol. 2001;330:445-54
pubmed: 11210523
PLoS One. 2011;6(6):e21624
pubmed: 21720566
Biochem Soc Trans. 2013 Feb 1;41(1):416-20
pubmed: 23356321
Nature. 1979 Feb 22;277(5698):667-9
pubmed: 423967
Bioinformation. 2015 Aug 31;11(8):413-5
pubmed: 26420923
Nature. 1986 Dec 18-31;324(6098):695-7
pubmed: 3540685
Biotechnology (N Y). 1995 Jul;13(7):662-8
pubmed: 9634802
Proteins. 2000 Mar 1;38(4):368-83
pubmed: 10707024
PLoS One. 2014 Apr 17;9(4):e93862
pubmed: 24743799
Science. 1995 Mar 10;267(5203):1463-9
pubmed: 7878465
BMC Bioinformatics. 2012 Jul 23;13:173
pubmed: 22823337
Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12300-5
pubmed: 9770481
Biochemistry. 2019 Mar 26;58(12):1616-1626
pubmed: 30786206
Structure. 1994 Dec 15;2(12):1157-67
pubmed: 7704526
J Mol Biol. 1992 Apr 20;224(4):1143-59
pubmed: 1569571
Bioinformation. 2014 Mar 19;10(3):164-6
pubmed: 24748757
Biochim Biophys Acta. 1987 Nov 26;916(2):200-4
pubmed: 3676331
Front Aging Neurosci. 2017 Feb 14;9:27
pubmed: 28261087
J Comput Chem. 2002 Apr 30;23(6):600-9
pubmed: 11939594
Protein Eng Des Sel. 2008 Dec;21(12):699-707
pubmed: 18836204
J Mol Biol. 1989 Mar 20;206(2):397-406
pubmed: 2716053
Bioinformation. 2015 Jul 31;11(7):366-8
pubmed: 26339154
Crit Rev Biochem Mol Biol. 2001;36(1):39-106
pubmed: 11256505
Bioinformation. 2015 Jan 30;11(1):39-42
pubmed: 25780279
J Biol Chem. 2019 Jan 4;294(1):89-100
pubmed: 30409909
Proteins. 2011 Apr;79(4):1089-108
pubmed: 21246632
Curr Opin Struct Biol. 1998 Dec;8(6):738-48
pubmed: 9914256