메뉴 건너뛰기




Volumn 1818, Issue 7, 2012, Pages 1595-1602

Interactions of the intact FsrC membrane histidine kinase with its pheromone ligand GBAP revealed through synchrotron radiation circular dichroism

Author keywords

FsrC; Gelatinase biosynthesis activating pheromone (GBAP); k d; Ligand interactions; Membrane histidine kinase; Synchrotron radiation circular dichroism

Indexed keywords

GELATINASE BIOSYNTHESIS ACTIVATING PHEROMONE; PHEROMONE; PROTEIN FSRC; PROTEIN HISTIDINE KINASE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

EID: 84859903462     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2012.02.015     Document Type: Article
Times cited : (23)

References (36)
  • 1
    • 9244249799 scopus 로고    scopus 로고
    • Hydrophobic interactions drive ligand-receptor recognition for activation and inhibition of staphylococcal quorum sensing
    • J.S. Wright III, G.J. Lyon, E.A. George, T.W. Muir, and R.P. Novick Hydrophobic interactions drive ligand-receptor recognition for activation and inhibition of staphylococcal quorum sensing Proc. Natl. Acad. Sci. U. S. A. 101 2004 16168 16173
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16168-16173
    • Wright Iii, J.S.1    Lyon, G.J.2    George, E.A.3    Muir, T.W.4    Novick, R.P.5
  • 2
    • 44049107495 scopus 로고    scopus 로고
    • Identification of ligand specificity determinants in AgrC, the Staphylococcus aureus quorum-sensing receptor
    • E. Geisinger, E.A. George, T.W. Muir, and R.P. Novick Identification of ligand specificity determinants in AgrC, the Staphylococcus aureus quorum-sensing receptor J. Biol. Chem. 283 2008 8930 8938
    • (2008) J. Biol. Chem. , vol.283 , pp. 8930-8938
    • Geisinger, E.1    George, E.A.2    Muir, T.W.3    Novick, R.P.4
  • 3
    • 47049112603 scopus 로고    scopus 로고
    • Differential recognition of Staphylococcus aureus quorum-sensing signals depends on both extracellular loops 1 and 2 of the transmembrane sensor AgrC
    • R.O. Jensen, K. Winzer, S.R. Clarke, W.C. Chan, and P. Williams Differential recognition of Staphylococcus aureus quorum-sensing signals depends on both extracellular loops 1 and 2 of the transmembrane sensor AgrC J. Mol. Biol. 381 2008 300 309
    • (2008) J. Mol. Biol. , vol.381 , pp. 300-309
    • Jensen, R.O.1    Winzer, K.2    Clarke, S.R.3    Chan, W.C.4    Williams, P.5
  • 4
    • 74249091562 scopus 로고    scopus 로고
    • Structural characterisation of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles
    • Y.P. Kim, K.J. Yeo, M.H. Kim, Y.-C. Kim, and Y.H. Jeon Structural characterisation of the intra-membrane histidine kinase YbdK from Bacillus subtilis in DPC micelles Biochem. Biophys. Res. Commun. 391 2010 1506 1511
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 1506-1511
    • Kim, Y.P.1    Yeo, K.J.2    Kim, M.H.3    Kim, Y.-C.4    Jeon, Y.H.5
  • 5
    • 53149107441 scopus 로고    scopus 로고
    • Expression and characterisation of the intergral membrane domain of bacterial histidine kinase SCO3062 for structural studies
    • K.J. Yeo, S.-N. Kwak, H.J. Kim, C. Cheong, M.H. Kim, and Y.H. Jeon Expression and characterisation of the intergral membrane domain of bacterial histidine kinase SCO3062 for structural studies Biochem. Biophys. Res. Commun. 376 2008 409 413
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 409-413
    • Yeo, K.J.1    Kwak, S.-N.2    Kim, H.J.3    Cheong, C.4    Kim, M.H.5    Jeon, Y.H.6
  • 8
    • 0036837964 scopus 로고    scopus 로고
    • Two-component signal transduction in Enterococcus faecalis
    • L.E. Hancock, and M. Perego Two-component signal transduction in Enterococcus faecalis J. Bacteriol. 184 2002 5819 5825
    • (2002) J. Bacteriol. , vol.184 , pp. 5819-5825
    • Hancock, L.E.1    Perego, M.2
  • 9
    • 0034946367 scopus 로고    scopus 로고
    • Gelatinase biosynthesis-activating pheromone: A peptide lactone that mediates a quorum sensing in Enterococcus faecalis
    • J. Nakayama, Y. Cao, T. Horii, S. Sakuda, A.D.L. Akkermans, W. de Vos, and H. Nagasawa Gelatinase biosynthesis-activating pheromone: a peptide lactone that mediates a quorum sensing in Enterococcus faecalis Mol. Microbiol. 41 2001 145 154
    • (2001) Mol. Microbiol. , vol.41 , pp. 145-154
    • Nakayama, J.1    Cao, Y.2    Horii, T.3    Sakuda, S.4    Akkermans, A.D.L.5    De Vos, W.6    Nagasawa, H.7
  • 10
    • 80052263187 scopus 로고    scopus 로고
    • Anti-HIV siamycin i directly inhibits autophosphorylation activity of the bacterial FsrC quorum sensor and other ATP-dependent enzyme activities
    • P. Ma, K. Nishiguchi, H.M. Yuille, L.M. Davis, J. Nakayama, and M.K. Phillips-Jones Anti-HIV siamycin I directly inhibits autophosphorylation activity of the bacterial FsrC quorum sensor and other ATP-dependent enzyme activities FEBS Lett. 585 2011 2660 2664
    • (2011) FEBS Lett. , vol.585 , pp. 2660-2664
    • Ma, P.1    Nishiguchi, K.2    Yuille, H.M.3    Davis, L.M.4    Nakayama, J.5    Phillips-Jones, M.K.6
  • 12
    • 78349254955 scopus 로고    scopus 로고
    • Measuring circular dichroism in a capillary cell using the B23 synchotron radiation CD beamline at Diamond Light Source
    • T. Javorfi, R. Hussain, D. Myatt, and G. Siligardi Measuring circular dichroism in a capillary cell using the B23 synchotron radiation CD beamline at Diamond Light Source Chirality 22 S1 2010 E149 E153
    • (2010) Chirality , vol.22 , Issue.S1
    • Javorfi, T.1    Hussain, R.2    Myatt, D.3    Siligardi, G.4
  • 14
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • S.W. Provencher, and J. Glockner Estimation of globular protein secondary structure from circular dichroism Biochemistry 20 1981 33 37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 16
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • N. Sreerama, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set Anal. Biochem. 287 2000 252 260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 17
    • 0346837919 scopus 로고    scopus 로고
    • Marine metabolites and metal chelation. CD studies of metal binding to Lissoclinum cyclopeptides
    • D.J. Freeman, G. Pattenden, A.F. Drake, and G. Siligardi Marine metabolites and metal chelation. CD studies of metal binding to Lissoclinum cyclopeptides J. Chem. Soc. Perkin Trans. 2 1998 129 135
    • (1998) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 129-135
    • Freeman, D.J.1    Pattenden, G.2    Drake, A.F.3    Siligardi, G.4
  • 18
    • 58649101393 scopus 로고    scopus 로고
    • Structure-activity relationship of gelatinase biosynthesis-activating pheromone of Enterococcus faecalis
    • K. Nishiguchi, K. Nagata, M. Tanokura, K. Sonomoto, and J. Nakayama Structure-activity relationship of gelatinase biosynthesis-activating pheromone of Enterococcus faecalis J. Bacteriol. 191 2009 641 650
    • (2009) J. Bacteriol. , vol.191 , pp. 641-650
    • Nishiguchi, K.1    Nagata, K.2    Tanokura, M.3    Sonomoto, K.4    Nakayama, J.5
  • 19
    • 0035490516 scopus 로고    scopus 로고
    • Chemical synthesis and biological activity of the gelatinase biosynthesis activating pheromone of Enterococcus faecalis and its analogs
    • J. Nakayama, Y. Cao, T. Horii, S. Sakuda, and H. Nagasawa Chemical synthesis and biological activity of the gelatinase biosynthesis activating pheromone of Enterococcus faecalis and its analogs Biosci. Biotechnol. Biochem. 65 2001 2322 2325
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2322-2325
    • Nakayama, J.1    Cao, Y.2    Horii, T.3    Sakuda, S.4    Nagasawa, H.5
  • 20
    • 0036296323 scopus 로고    scopus 로고
    • Expression, purification and characterisation of the full-length histidine protein kinase RegB from Rhodobacter sphaeroides
    • C.A. Potter, A. Ward, C. Laguri, M.P. Williamson, P.J.F. Henderson, and M.K. Phillips-Jones Expression, purification and characterisation of the full-length histidine protein kinase RegB from Rhodobacter sphaeroides J. Mol. Biol. 320 2002 201 213
    • (2002) J. Mol. Biol. , vol.320 , pp. 201-213
    • Potter, C.A.1    Ward, A.2    Laguri, C.3    Williamson, M.P.4    Henderson, P.J.F.5    Phillips-Jones, M.K.6
  • 22
    • 80054687050 scopus 로고    scopus 로고
    • Toward rational design of protein detergent complexes: Determinants of mixed micelles that are critical for the in vitro stabilisation of a G-protein coupled receptor
    • M.A. O'Malley, M.E. Helgeson, N.J. Wagner, and A.S. Robinson Toward rational design of protein detergent complexes: determinants of mixed micelles that are critical for the in vitro stabilisation of a G-protein coupled receptor Biophys. J. 101 2011 1938 1948
    • (2011) Biophys. J. , vol.101 , pp. 1938-1948
    • O'Malley, M.A.1    Helgeson, M.E.2    Wagner, N.J.3    Robinson, A.S.4
  • 24
    • 0028211897 scopus 로고
    • Correlations between biological activities and conformational properties of human, salmon, eel, porcine calcitonin and elcatonin elucidated by Circular Dichroism spectroscopy
    • G. Siligardi, B. Samori, S. Melandri, M. Visconti, and A.F. Drake Correlations between biological activities and conformational properties of human, salmon, eel, porcine calcitonin and elcatonin elucidated by Circular Dichroism spectroscopy Eur. J. Biochem. 221 1994 1117 1125
    • (1994) Eur. J. Biochem. , vol.221 , pp. 1117-1125
    • Siligardi, G.1    Samori, B.2    Melandri, S.3    Visconti, M.4    Drake, A.F.5
  • 25
    • 77950496251 scopus 로고    scopus 로고
    • Practical considerations of membrane protein instability during purification and crystallisation
    • C.G. Tate Practical considerations of membrane protein instability during purification and crystallisation Methods Mol. Biol. 601 2010 187 203
    • (2010) Methods Mol. Biol. , vol.601 , pp. 187-203
    • Tate, C.G.1
  • 26
    • 80051996587 scopus 로고    scopus 로고
    • NMR structures of polytopic integral membrane proteins
    • S.G. Patching NMR structures of polytopic integral membrane proteins Mol. Membr. Biol. 28 2011 370 397
    • (2011) Mol. Membr. Biol. , vol.28 , pp. 370-397
    • Patching, S.G.1
  • 27
    • 52049091255 scopus 로고    scopus 로고
    • The effects of lipids on the structure of the eukaryotic cytolysin equinatoxin II: A synchotron radiation circular dichroism spectrscopic study
    • A.J. Miles, A. Drechsler, K. Kristan, G. Anderluh, R.S. Norton, B.A. Wallace, and F. Separovic The effects of lipids on the structure of the eukaryotic cytolysin equinatoxin II: a synchotron radiation circular dichroism spectrscopic study Biochim. Biophys. Acta 1778 2008 2091 2096
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2091-2096
    • Miles, A.J.1    Drechsler, A.2    Kristan, K.3    Anderluh, G.4    Norton, R.S.5    Wallace, B.A.6    Separovic, F.7
  • 30
    • 78149448781 scopus 로고    scopus 로고
    • Discovery of biphasic thermal unfolding of OmpC with implications for surface loop stability
    • N. Keegan, H. Ridley, and J.H. Lakey Discovery of biphasic thermal unfolding of OmpC with implications for surface loop stability Biochemistry 49 2010 9715 9721
    • (2010) Biochemistry , vol.49 , pp. 9715-9721
    • Keegan, N.1    Ridley, H.2    Lakey, J.H.3
  • 31
    • 34247401600 scopus 로고    scopus 로고
    • Temperature and urea induced conformational changes of the histidine kinases from Mycobacterium tuberculosis
    • R. Shrivastava, and A.K. Das Temperature and urea induced conformational changes of the histidine kinases from Mycobacterium tuberculosis Int. J. Biol. Macromol. 41 2007 154 161
    • (2007) Int. J. Biol. Macromol. , vol.41 , pp. 154-161
    • Shrivastava, R.1    Das, A.K.2
  • 32
    • 79959922924 scopus 로고    scopus 로고
    • Spectroscopic analysis of the intrinsic chromophores within small multidrug resistance protein SugE
    • D.C. Bay, and R.J. Turner Spectroscopic analysis of the intrinsic chromophores within small multidrug resistance protein SugE Biochim. Biophys. Acta 1808 2011 2233 2244
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2233-2244
    • Bay, D.C.1    Turner, R.J.2
  • 34
    • 0038290306 scopus 로고    scopus 로고
    • Identification of basic amino acids important for citrate binding by the periplasmic receptor domain of the sensor kinase CitA
    • T. Gerharz, S. Reinelt, S. Kaspar, L. Scapozza, and M. Bott Identification of basic amino acids important for citrate binding by the periplasmic receptor domain of the sensor kinase CitA Biochemistry 42 2003 5917 5924
    • (2003) Biochemistry , vol.42 , pp. 5917-5924
    • Gerharz, T.1    Reinelt, S.2    Kaspar, S.3    Scapozza, L.4    Bott, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.