메뉴 건너뛰기




Volumn 2, Issue , 2012, Pages 173-177

Exploring potassium-dependent GTP hydrolysis in TEES family GTPases

Author keywords

GTPases; HAS GTPases; Hydrolysis mechanism; K+ stimulated hydrolysis; K loop

Indexed keywords

ASPARAGINE; DYNAMIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; POTASSIUM ION; SODIUM ION; TEES GUANOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 84867325780     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2012.07.008     Document Type: Article
Times cited : (13)

References (22)
  • 1
    • 0026026818 scopus 로고
    • The GTPase superfamily: conserved structure and molecular mechanism
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 1991, 349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol 2002, 317:41-72.
    • (2002) J. Mol. Biol , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 3
    • 0025010979 scopus 로고
    • The GTPase superfamily: a conserved switch for diverse cell functions
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 1990, 348:125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 4
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • Wittinghofer A., Vetter I.R. Structure-function relationships of the G domain, a canonical switch motif. Annu. Rev. Biochem 2011, 80:943-971.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 6
    • 0030036699 scopus 로고    scopus 로고
    • Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins
    • Mittal R., Ahmadian M.R., Goody R.S., Wittinghofer A. Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins. Science 1996, 273:115-117.
    • (1996) Science , vol.273 , pp. 115-117
    • Mittal, R.1    Ahmadian, M.R.2    Goody, R.S.3    Wittinghofer, A.4
  • 7
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: helping hands to complement an active site
    • Scheffzek K., Ahmadian M.R., Wittinghofer A. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci 1998, 23:257-262.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 8
    • 16344363783 scopus 로고    scopus 로고
    • Analysis of GTPases carrying hydrophobic amino acid substitutions in lieu of the catalytic glutamine: Implications for GTP hydrolysis
    • Mishra R., Gara S.K., Mishra S., Prakash B. Analysis of GTPases carrying hydrophobic amino acid substitutions in lieu of the catalytic glutamine: Implications for GTP hydrolysis. Proteins-Struct. Funct. Bioinformat 2005, 59:332-338.
    • (2005) Proteins-Struct. Funct. Bioinformat , vol.59 , pp. 332-338
    • Mishra, R.1    Gara, S.K.2    Mishra, S.3    Prakash, B.4
  • 9
    • 33745520400 scopus 로고    scopus 로고
    • Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element
    • Scrima A., Wittinghofer A. Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element. EMBO J. 2006, 25:2940-2951.
    • (2006) EMBO J. , vol.25 , pp. 2940-2951
    • Scrima, A.1    Wittinghofer, A.2
  • 10
    • 77956326447 scopus 로고    scopus 로고
    • Deciphering the catalytic machinery in 30S ribosome assembly GTPase YqeH
    • Anand B., Surana P., Prakash B. Deciphering the catalytic machinery in 30S ribosome assembly GTPase YqeH. PLoS One 2010, 5:e9944.
    • (2010) PLoS One , vol.5
    • Anand, B.1    Surana, P.2    Prakash, B.3
  • 11
    • 77951980333 scopus 로고    scopus 로고
    • Potassium-activated GTPase reaction in the G protein-coupled ferrous iron transporter B
    • Ash M.R., Guilfoyle A., Clarke R.J., Guss J.M., Maher M.J., Jormakka M. Potassium-activated GTPase reaction in the G protein-coupled ferrous iron transporter B. J. Biol. Chem 2010, 285:14594-14602.
    • (2010) J. Biol. Chem , vol.285 , pp. 14594-14602
    • Ash, M.R.1    Guilfoyle, A.2    Clarke, R.J.3    Guss, J.M.4    Maher, M.J.5    Jormakka, M.6
  • 12
    • 84858013820 scopus 로고    scopus 로고
    • Biochemical characterization of the ribosome assembly GTPase RbgA in Bacillus subtilis
    • Achila D., Gulati M., Jain N., Britton R.A. Biochemical characterization of the ribosome assembly GTPase RbgA in Bacillus subtilis. J. Biol. Chem 2012, 287:8417-8423.
    • (2012) J. Biol. Chem , vol.287 , pp. 8417-8423
    • Achila, D.1    Gulati, M.2    Jain, N.3    Britton, R.A.4
  • 13
    • 0037418665 scopus 로고    scopus 로고
    • Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)(14) at 2.0 angstrom resolution
    • Wang J., Boisvert D.C. Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)(14) at 2.0 angstrom resolution. J. Mol. Biol 2003, 327:843-855.
    • (2003) J. Mol. Biol , vol.327 , pp. 843-855
    • Wang, J.1    Boisvert, D.C.2
  • 14
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks S.M., McKay D.B. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem 1995, 270:2251-2257.
    • (1995) J. Biol. Chem , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 15
    • 79955759612 scopus 로고    scopus 로고
    • Deciphering the catalytic machinery in a universally conserved ribosome binding ATPase YchF
    • Tomar S.K., Kumar P., Prakash B. Deciphering the catalytic machinery in a universally conserved ribosome binding ATPase YchF. Biochem. Biophys. Res. Commun 2011, 408:459-464.
    • (2011) Biochem. Biophys. Res. Commun , vol.408 , pp. 459-464
    • Tomar, S.K.1    Kumar, P.2    Prakash, B.3
  • 16
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie J.S., Acharya S., Leonard M., Schmid S.L., Dyda F. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 2010, 465:435-440.
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 19
    • 84856063603 scopus 로고    scopus 로고
    • Structural basis for GTP-dependent dimerization of hydrogenase maturation factor HypB
    • Chan K.-H., Li T., Wong C.-O., Wong K.-B. Structural basis for GTP-dependent dimerization of hydrogenase maturation factor HypB. Plos ONE 2012, 7:e30547.
    • (2012) Plos ONE , vol.7
    • Chan, K.-H.1    Li, T.2    Wong, C.-O.3    Wong, K.-B.4
  • 20
    • 1842848075 scopus 로고    scopus 로고
    • Domain arrangement of Der, a switch protein containing two GTPase domains
    • Robinson V.L., Hwang J., Fox E., Inouye M., Stock A.M. Domain arrangement of Der, a switch protein containing two GTPase domains. Structure 2002, 10:1649-1658.
    • (2002) Structure , vol.10 , pp. 1649-1658
    • Robinson, V.L.1    Hwang, J.2    Fox, E.3    Inouye, M.4    Stock, A.M.5
  • 21
    • 33747584905 scopus 로고    scopus 로고
    • The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding
    • Muench S.P., Xu L., Sedelnikova S.E., Rice D.W. The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding. Proc. Natl. Acad. Sci. U S A 2006, 103:12359-12364.
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 12359-12364
    • Muench, S.P.1    Xu, L.2    Sedelnikova, S.E.3    Rice, D.W.4
  • 22
    • 65549102208 scopus 로고    scopus 로고
    • Distinct GDP/GTP bound states of the tandem G-domains of EngA regulate ribosome binding
    • Tomar S.K., Dhimole N., Chatterjee M., Prakash B. Distinct GDP/GTP bound states of the tandem G-domains of EngA regulate ribosome binding. Nucleic Acids Res 2009, 37:2359-2370.
    • (2009) Nucleic Acids Res , vol.37 , pp. 2359-2370
    • Tomar, S.K.1    Dhimole, N.2    Chatterjee, M.3    Prakash, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.