메뉴 건너뛰기




Volumn 34, Issue 4, 2014, Pages 357-368

Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice

Author keywords

Bacterial Ig like fold; Crystal structure; Extender domain; Ice binding adhesin; Solution structure

Indexed keywords

BACTERIAL PROTEIN; CALCIUM; ICE; IMMUNOGLOBULIN; OXYGEN; PROTEIN BINDING;

EID: 84906835738     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20140083     Document Type: Article
Times cited : (34)

References (43)
  • 2
    • 80053286819 scopus 로고    scopus 로고
    • Structure and function of MARTX toxins and other large repetitive RTX proteins
    • CrossRef PubMed
    • Satchell, K. J. (2011) Structure and function of MARTX toxins and other large repetitive RTX proteins. Annu. Rev. Microbiol. 65, 71-90 CrossRef PubMed
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 71-90
    • Satchell, K.J.1
  • 3
    • 77954843913 scopus 로고    scopus 로고
    • LapF, the second largest Pseudomonas putida protein, contributes to plant root colonization and determines biofilm architecture
    • CrossRef PubMed
    • Martinez-Gil, M., Yousef-Coronado, F. and Espinosa-Urgel, M. (2010) LapF, the second largest Pseudomonas putida protein, contributes to plant root colonization and determines biofilm architecture. Mol. Microbiol. 77, 549-561 CrossRef PubMed
    • (2010) Mol. Microbiol. , vol.77 , pp. 549-561
    • Martinez-Gil, M.1    Yousef-Coronado, F.2    Espinosa-Urgel, M.3
  • 4
    • 0034005123 scopus 로고    scopus 로고
    • Genetic analysis of functions involved in adhesion of Pseudomonas putida to seeds
    • DOI 10.1128/JB.182.9.2363-2369.2000
    • Espinosa-Urgel, M., Salido, A. and Ramos, J. L. (2000) Genetic analysis of functions involved in adhesion of Pseudomonas putida to seeds. J. Bacteriol. 182, 2363-2369 CrossRef PubMed (Pubitemid 30212890)
    • (2000) Journal of Bacteriology , vol.182 , Issue.9 , pp. 2363-2369
    • Espinosa-Urgel, M.1    Salido, A.2    Ramos, J.-L.3
  • 5
    • 84877576585 scopus 로고    scopus 로고
    • Structural insight into the giant Ca(2) (+) -binding adhesin SiiE: Implications for the adhesion of Salmonella enterica to polarized epithelial cells
    • CrossRef PubMed
    • Griessl, M. H., Schmid, B., Kassler, K., Braunsmann, C., Ritter, R., Barlag, B., Stierhof, Y. D., Sturm, K. U., Danzer, C., Wagner, C. et al. (2013) Structural insight into the giant Ca(2) (+) -binding adhesin SiiE: implications for the adhesion of Salmonella enterica to polarized epithelial cells. Structure 21, 741-752 CrossRef PubMed
    • (2013) Structure , vol.21 , pp. 741-752
    • Griessl, M.H.1    Schmid, B.2    Kassler, K.3    Braunsmann, C.4    Ritter, R.5    Barlag, B.6    Stierhof, Y.D.7    Sturm, K.U.8    Danzer, C.9    Wagner, C.10
  • 6
    • 70350462611 scopus 로고    scopus 로고
    • The Vibrio cholerae flagellar regulatory hierarchy controls expression of virulence factors
    • CrossRef PubMed
    • Syed, K. A., Beyhan, S., Correa, N., Queen, J., Liu, J., Peng, F., Satchell, K. J., Yildiz, F. and Klose, K. E. (2009) The Vibrio cholerae flagellar regulatory hierarchy controls expression of virulence factors. J. Bacteriol. 191, 6555-6570 CrossRef PubMed
    • (2009) J. Bacteriol. , vol.191 , pp. 6555-6570
    • Syed, K.A.1    Beyhan, S.2    Correa, N.3    Queen, J.4    Liu, J.5    Peng, F.6    Satchell, K.J.7    Yildiz, F.8    Klose, K.E.9
  • 7
    • 15744400083 scopus 로고    scopus 로고
    • 2+-dependent antifreeze protein in an Antarctic bacterium
    • DOI 10.1016/j.femsle.2005.02.022
    • Gilbert, J. A., Davies, P. L. and Laybourn-Parry, J. (2005) A hyperactive, Ca2 + -dependent antifreeze protein in an Antarctic bacterium. FEMS Microbiol. Lett. 245, 67-72 CrossRef PubMed (Pubitemid 40410678)
    • (2005) FEMS Microbiology Letters , vol.245 , Issue.1 , pp. 67-72
    • Gilbert, J.A.1    Davies, P.L.2    Laybourn-Parry, J.3
  • 9
    • 84868686533 scopus 로고    scopus 로고
    • Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity
    • CrossRef PubMed
    • Guo, S. Q., Garnham, C. P., Whitney, J. C., Graham, L. A. and Davies, P. L. (2012) Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. PLoS ONE 7, e48805 CrossRef PubMed
    • (2012) PLoS ONE , vol.7
    • Guo, S.Q.1    Garnham, C.P.2    Whitney, J.C.3    Graham, L.A.4    Davies, P.L.5
  • 10
    • 79956332670 scopus 로고    scopus 로고
    • Anchored clathrate waters bind antifreeze proteins to ice
    • CrossRef PubMed
    • Garnham, C. P., Campbell, R. L. and Davies, P. L. (2011) Anchored clathrate waters bind antifreeze proteins to ice. Proc. Natl. Acad. Sci. U.S.A. 108, 7363-7367 CrossRef PubMed
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 7363-7367
    • Garnham, C.P.1    Campbell, R.L.2    Davies, P.L.3
  • 11
    • 33845661120 scopus 로고    scopus 로고
    • Beta-Rolls, beta-Helices, and Other beta-Solenoid Proteins
    • DOI 10.1016/S0065-3233(06)73003-0, PII S0065323306730030, Fibrous Proteins: Amyloids, Prions and Beta Proteins
    • Kajava, A. V. and Steven, A. C. (2006) Beta-rolls, beta-helices, and other beta-solenoid proteins. Adv. Protein Chem. 73, 55-96 CrossRef PubMed (Pubitemid 44960401)
    • (2006) Advances in Protein Chemistry , vol.73 , pp. 55-96
    • Kajava, A.V.1    Steven, A.C.2
  • 13
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • CrossRef PubMed
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606-1619 CrossRef PubMed
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 14
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • CrossRef PubMed
    • Kabsch, W. (2010) Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144 CrossRef PubMed
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 15
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • CrossRef
    • Evans, P. R. (2006) Scaling and assessment of data quality. Acta Crystallogr. D 62, 72-82 CrossRef
    • (2006) Acta Crystallogr. D , vol.62 , pp. 72-82
    • Evans, P.R.1
  • 18
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • CrossRef PubMed
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011 CrossRef PubMed
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 23
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • CrossRef PubMed
    • Painter, J. and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr. D Biol. Crystallogr. 62, 439-450 CrossRef PubMed
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 25
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • DOI 10.1107/S002188980700252X, PII S002188980700252X
    • Mylonas, E. and Svergun, D. I. (2007) Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. J. Appl. Crystallogr. 40, S245-S249 CrossRef (Pubitemid 46732696)
    • (2007) Journal of Applied Crystallography , vol.40 , Issue.SUPPL. 1
    • Mylonas, E.1    Svergun, D.I.2
  • 26
    • 0141484613 scopus 로고    scopus 로고
    • PRIMUS: A Windows PC-based system for small-angle scattering data analysis
    • CrossRef
    • Konarev, P. V., Volkov, V. V., Sokolova, A. V., Koch, M. H. J. and Svergun, D. I. (2003) PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J. Appl. Crystallogr. 36, 1277-1282 CrossRef
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 1277-1282
    • Konarev, P.V.1    Volkov, V.V.2    Sokolova, A.V.3    Koch, M.H.J.4    Svergun, D.I.5
  • 27
    • 0030569147 scopus 로고    scopus 로고
    • Scattering functions of semiflexible polymers with and without excluded volume effects
    • CrossRef
    • Pedersen, J. S. and Schurtenberger, P. (1996) Scattering functions of semiflexible polymers with and without excluded volume effects. Macromolecules 29, 7602-7612 CrossRef
    • (1996) Macromolecules , vol.29 , pp. 7602-7612
    • Pedersen, J.S.1    Schurtenberger, P.2
  • 28
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • CrossRef PubMed
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886 CrossRef PubMed
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 29
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • CrossRef
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503 CrossRef
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 30
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • CrossRef
    • Volkov, V. V. and Svergun, D. I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864 CrossRef
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 32
    • 77649270954 scopus 로고    scopus 로고
    • Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy
    • CrossRef
    • Erickson, H. P. (2009) Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol. Proc. Online 11, 32-51 CrossRef
    • (2009) Biol. Proc. Online , vol.11 , pp. 32-51
    • Erickson, H.P.1
  • 34
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D. I., Barberato, C. and Koch, M. H. J. (1995) CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773 CrossRef (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 35
    • 0036470053 scopus 로고    scopus 로고
    • Antifreeze proteins: An unusual receptor-ligand interaction
    • DOI 10.1016/S0968-0004(01)02028-X, PII S096800040102028X
    • Jia, Z. and Davies, P. L. (2002) Antifreeze proteins: an unusual receptor-ligand interaction. Trends Biochem. Sci. 27, 101-106 CrossRef PubMed (Pubitemid 34164326)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.2 , pp. 101-106
    • Jia, Z.1    Davies, P.L.2
  • 36
    • 0002364934 scopus 로고    scopus 로고
    • The Chemical Stratification and Microbial Communities of Ace Lake, Antarctica: A Review of the Characteristics of a Marine-Derived Meromictic Lake
    • Rankin, L. M., Gibson, J. A. E., Franzmann, P. D. and Burton, H. R. (1999) The chemical stratification and microbial communities of Ace Lake, Antarctica: a review of the characteristics of a marine-derived Meromictic lake. Polarforschung 66, 33-52 (Pubitemid 126431288)
    • (1996) Polarforschung , vol.66 , Issue.1 , pp. 33-52
    • Rankin, L.M.1    Gibson, J.A.E.2    Franzmann, P.D.3    Burton, H.R.4
  • 37
    • 1642473904 scopus 로고    scopus 로고
    • Demonstration of antifreeze protein activity in Antarctic lake bacteria
    • Gilbert, J. A., Hill, P. J., Dodd, C. E. and Laybourn-Parry, J. (2004) Demonstration of antifreeze protein activity in Antarctic lake bacteria. Microbiology 150, 171-180 CrossRef PubMed (Pubitemid 38111483)
    • (2004) Microbiology , vol.150 , Issue.1 , pp. 171-180
    • Gilbert, J.A.1    Hill, P.J.2    Dodd, C.E.R.3    Laybourn-Parry, J.4
  • 38
    • 77954634710 scopus 로고    scopus 로고
    • Antifreeze proteins in polar sea ice diatoms: Diversity and gene expression in the genus Fragilariopsis
    • CrossRef PubMed
    • Bayer-Giraldi, M., Uhlig, C., John, U., Mock, T. and Valentin, K. (2010) Antifreeze proteins in polar sea ice diatoms: diversity and gene expression in the genus Fragilariopsis. Environ. Microbiol. 12, 1041-1052 CrossRef PubMed
    • (2010) Environ. Microbiol. , vol.12 , pp. 1041-1052
    • Bayer-Giraldi, M.1    Uhlig, C.2    John, U.3    Mock, T.4    Valentin, K.5
  • 40
    • 60149111839 scopus 로고    scopus 로고
    • Pili in Gram-negative and Gram-positive bacteria-structure, assembly and their role in disease
    • CrossRef PubMed
    • Proft, T. and Baker, E. N. (2009) Pili in Gram-negative and Gram-positive bacteria-structure, assembly and their role in disease. Cell. Mol. Life Sci. 66, 613-635 CrossRef PubMed
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 613-635
    • Proft, T.1    Baker, E.N.2
  • 41
    • 0036188648 scopus 로고    scopus 로고
    • Rational design of alpha-helical antifreeze peptides
    • DOI 10.1046/j.1397-002x.2001.00001.x
    • Kuiper, M. J., Fecondo, J. V. and Wong, M. G. (2002) Rational design of alpha-helical antifreeze peptides. J. Pept. Res. 59, 1-8 CrossRef PubMed (Pubitemid 34185255)
    • (2002) Journal of Peptide Research , vol.59 , Issue.1 , pp. 1-8
    • Kuiper, M.J.1    Fecondo, J.V.2    Wong, M.G.3
  • 43
    • 77950223101 scopus 로고    scopus 로고
    • Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls
    • CrossRef PubMed
    • Jacques, D. A. and Trewhella, J. (2010) Small-angle scattering for structural biology-expanding the frontier while avoiding the pitfalls. Protein Sci. 19, 642-657 CrossRef PubMed
    • (2010) Protein Sci. , vol.19 , pp. 642-657
    • Jacques, D.A.1    Trewhella, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.