메뉴 건너뛰기




Volumn 26, Issue 9, 2001, Pages 550-557

Ion pairs and the thermotolerance of proteins from hyperthermophiles: A 'traffic rule' for hot roads

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0035448574     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(01)01918-1     Document Type: Review
Times cited : (274)

References (34)
  • 1
    • 0030596013 scopus 로고    scopus 로고
    • Thermal unfolding of the DNA-binding protein Sso7d from hyperthermophile Sulfolobus solfataricus
    • (1996) J. Mol. Biol. , vol.264 , pp. 1132-1144
    • Knapp, S.1
  • 2
    • 0026648514 scopus 로고
    • Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    • (1992) J. Biol. Chem. , vol.267 , pp. 10999-11006
    • Rehaber, V.1
  • 4
    • 0031567156 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus
    • (1997) J. Mol. Biol. , vol.266 , pp. 1016-1031
    • Wallon, G.1
  • 6
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • (1995) Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1
  • 7
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1
  • 8
    • 0035830969 scopus 로고    scopus 로고
    • X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 Å resolution: Determinants of thermostability revealed from structural comparisons
    • (2001) J. Mol. Biol. , vol.306 , pp. 1099-1114
    • Zhang, X.1
  • 9
    • 0027156651 scopus 로고
    • Determinants of protein stability in the 1.9 Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • (1993) Biochemistry , vol.32 , pp. 3913-3922
    • Kelly, C.A.1
  • 10
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1
  • 11
    • 0031564613 scopus 로고    scopus 로고
    • Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 2.5 Å resolution
    • (1997) J. Mol. Biol. , vol.267 , pp. 916-932
    • Knapp, S.1
  • 12
    • 0028903461 scopus 로고    scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • (1997) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1
  • 13
    • 0031816805 scopus 로고    scopus 로고
    • A protein disulfide oxidoreductese from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 602-611
    • Ren, B.1
  • 14
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.P.1
  • 15
    • 0032528267 scopus 로고    scopus 로고
    • Insights into the molecular basis of thermal stability from the analysis of ion-pair networks in the glutamate dehydrogenase family
    • (1998) Eur. J. Biochem. , vol.255 , pp. 336-346
    • Yip, K.S.P.1
  • 17
    • 0027246520 scopus 로고
    • Crystal structure of ribonuclease H from Thermus thermophilus HB8 refined at 2.8 Å resolution
    • (1993) J. Mol. Biol. , vol.230 , pp. 592-542
    • Ishikawa, K.1
  • 18
    • 0030977659 scopus 로고    scopus 로고
    • Crystal structure at 2.0 Å resolution of phosphoribosil anthranilate isomerase from the hyperthermophile Thetmotoga maritima: Possible determinants of protein stability
    • (1997) Biochemistry , vol.36 , pp. 6009-6016
    • Henning, M.1
  • 19
    • 0025126043 scopus 로고
    • Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1
  • 20
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1104
    • Horovitz, A.1
  • 21
    • 0031723935 scopus 로고    scopus 로고
    • Crystal structure of rubredoxin from Pyrococcus furiosus at 0.95 Å resolution, and the structures of N-terminal methionine and formylmethionine variants of Pf Rd. Contributions of N-terminal interactions to thermostability
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 484-493
    • Bau, R.1
  • 22
    • 0034673153 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability
    • (2000) Biochemistry , vol.39 , pp. 1251-1255
    • Strop, P.1
  • 24
    • 0033523004 scopus 로고    scopus 로고
    • Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: Construction of a 16-residue ion pair network at the subunit interface
    • (1999) J. Mol. Biol. , vol.289 , pp. 357-369
    • Lebbink, J.H.G.1
  • 25
    • 0344609869 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the hyperthermophilic protein Sac7d from Sulfolobus acidocaldarius: Contributions of salt bridges to thermostability
    • (1999) J. Mol. Biol. , vol.28 , pp. 1811-1830
    • De Bakker, P.I.W.1
  • 26
    • 0032502317 scopus 로고    scopus 로고
    • Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins
    • (1998) Biochemistry , vol.37 , pp. 3369-3376
    • Cavagnero, S.1
  • 28
    • 0028126676 scopus 로고
    • The optimisation of the electrostatic interactions in proteins of different functional and folding type
    • (1994) Protein Sci. , vol.3 , pp. 1556-1569
    • Spassov, V.Z.1
  • 30
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures - Implications for hyperthermophilic proteins
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 32
    • 0029115963 scopus 로고
    • The optimization of protein solvent interactions. Thermostability and the role of hydrophobic and electrostatic interactions
    • (1995) Protein Sci. , vol.4 , pp. 1516-1527
    • Spassov, V.Z.1
  • 33
    • 0030926503 scopus 로고    scopus 로고
    • Optimization of the electrostatic interactions between ionized groups and peptide dipoles in proteins
    • (1997) Protein Sci. , vol.6 , pp. 1190-1195
    • Spassov, V.Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.