메뉴 건너뛰기




Volumn 277, Issue 13, 2010, Pages 2868-2882

Crystal structure determination and inhibition studies of a novel xylanase and α-amylase inhibitor protein (XAIP) from Scadoxus multiflorus

Author keywords

Amylase; Crystal structure; Enzyme inhibition; TIM barrel fold; Xylanase

Indexed keywords

AMYLASE; AMYLASE INHIBITOR; CARBOHYDRATE BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; POLYPEPTIDE; PROTEIN; PROTEIN XAIP; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 77953599240     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07703.x     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 33746220462 scopus 로고    scopus 로고
    • Plant protein inhibitors of cell wall degrading enzymes
    • Juge N (2006) Plant protein inhibitors of cell wall degrading enzymes. Trends Plant Sci 11, 359-367.
    • (2006) Trends Plant Sci , vol.11 , pp. 359-367
    • Juge, N.1
  • 3
    • 48049120629 scopus 로고    scopus 로고
    • Enzyme-inhibitor interactions at the plant-pathogen interface
    • Misas-Villamil JC van der Hoorn RA (2008) Enzyme-inhibitor interactions at the plant-pathogen interface. Curr Opin Struct Biol 11, 380-388.
    • (2008) Curr Opin Struct Biol , vol.11 , pp. 380-388
    • Misas-Villamil, J.C.1    Van Der Hoorn, R.A.2
  • 4
    • 0002625707 scopus 로고
    • A pectin lyase inhibitor protein from cell-walls of sugar-beet
    • Bugbee WM (1993) A pectin lyase inhibitor protein from cell-walls of sugar-beet. Phytopathology 83, 63-68.
    • (1993) Phytopathology , vol.83 , pp. 63-68
    • Bugbee, W.M.1
  • 9
  • 10
    • 0030595119 scopus 로고    scopus 로고
    • The 1.8 ̊ resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18
    • Vanscheltinga ACT, Hennig M Dijkstra BW (1996) The 1.8 ̊ resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18. J Mol Biol 262, 243-257.
    • (1996) J Mol Biol , vol.262 , pp. 243-257
    • Vanscheltinga, A.C.T.1    Hennig, M.2    Dijkstra, B.W.3
  • 11
    • 0028845991 scopus 로고
    • Crystal structure of concanavalin B at 1.65 ̊ resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis
    • Hennig M, Jansonius JN, Vanscheltinga ACT, Dijkstra BW Schlesier B (1995) Crystal structure of concanavalin B at 1.65 ̊ resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis. J Mol Biol 254, 237-246.
    • (1995) J Mol Biol , vol.254 , pp. 237-246
    • Hennig, M.1    Jansonius, J.N.2    Vanscheltinga, A.C.T.3    Dijkstra, B.W.4    Schlesier, B.5
  • 13
    • 0038677006 scopus 로고    scopus 로고
    • Structural analysis of xylanase inhibitor protein I (XIP-I), a proteinaceous xylanase inhibitor from wheat (Triticum aestivum var. Soisson)
    • Payan F, Flatman R, Porciero S, Williamson G, Juge N Roussel A (2003) Structural analysis of xylanase inhibitor protein I (XIP-I), a proteinaceous xylanase inhibitor from wheat (Triticum aestivum var. Soisson). Biochem J 372, 399-405.
    • (2003) Biochem J , vol.372 , pp. 399-405
    • Payan, F.1    Flatman, R.2    Porciero, S.3    Williamson, G.4    Juge, N.5    Roussel, A.6
  • 14
    • 0037832147 scopus 로고    scopus 로고
    • Protein informatics towards function identification
    • Kengo K Haruki N (2003) Protein informatics towards function identification. Curr Opin Struct Biol 13, 396-400.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 396-400
    • Kengo, K.1    Haruki, N.2
  • 15
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • Farber GK Petsko GA (1990) The evolution of α/β barrel enzymes. Trends Biochem Sci 15, 228-234.
    • (1990) Trends Biochem Sci , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 16
    • 0028774717 scopus 로고
    • Crystal structure of a bacterial chitinase at 2.3 ̊ resolution
    • Wilson KS Vorgias CE (1994) Crystal structure of a bacterial chitinase at 2.3 ̊ resolution. Structure 2, 1169-1180.
    • (1994) Structure , vol.2 , pp. 1169-1180
    • Wilson, K.S.1    Vorgias, C.E.2
  • 17
    • 0001053032 scopus 로고
    • New substrates for use with chitinases
    • Hackman RH Goldberg M (1964) New substrates for use with chitinases. Anal Biochem 8, 397-401.
    • (1964) Anal Biochem , vol.8 , pp. 397-401
    • Hackman, R.H.1    Goldberg, M.2
  • 18
    • 0037837789 scopus 로고    scopus 로고
    • Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface
    • Machius M, Declerck N, Huber R Wiegand G (2003) Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface. J Biol Chem 278, 11546-11553.
    • (2003) J Biol Chem , vol.278 , pp. 11546-11553
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 19
    • 0037361621 scopus 로고    scopus 로고
    • A wheat xylanase inhibitor protein (XIP-I) accumulates in the grain and has homologues in other cereals
    • Elliott GO, McLauchlan WR, Williamson G Kroon PA (2003) A wheat xylanase inhibitor protein (XIP-I) accumulates in the grain and has homologues in other cereals. J Cereal Sci 2, 187-194.
    • (2003) J Cereal Sci , vol.2 , pp. 187-194
    • Elliott, G.O.1    McLauchlan, W.R.2    Williamson, G.3    Kroon, P.A.4
  • 22
    • 77953580353 scopus 로고    scopus 로고
    • access date: March 10
    • http://linux.softberry.com/berry.phtml? access date: March 10, 2010.
    • (2010)
  • 25
  • 26
    • 0029644724 scopus 로고
    • Crystal structure of endo-b-N-acetylglucosaminidase H at 1.9 ̊ resolution: Active-site geometry and substrate recognition
    • Rao VH, Guan C van Roey P (1995) Crystal structure of endo-b-N-acetylglucosaminidase H at 1.9 ̊ resolution: active-site geometry and substrate recognition. Structure 3, 449-457.
    • (1995) Structure , vol.3 , pp. 449-457
    • Rao, V.H.1    Guan, C.2    Van Roey, P.3
  • 27
    • 0032524130 scopus 로고    scopus 로고
    • Barley alpha-amylase bound to its endogenous protein inhibitor BASI: Crystal structure of the complex at 1.9 ̊ resolution
    • Vallee F, Kadziola A, Bourne Y, Juy M, Rodenburg KW, Svensson B Haser R (1998) Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 ̊ resolution. Structure 15, 649-659.
    • (1998) Structure , vol.15 , pp. 649-659
    • Vallee, F.1    Kadziola, A.2    Bourne, Y.3    Juy, M.4    Rodenburg, K.W.5    Svensson, B.6    Haser, R.7
  • 28
    • 33751346581 scopus 로고    scopus 로고
    • Plant α-amylase: Functions and role in carbohydrate metabolism
    • Stanley D, Farnden FJK Macrae AE (2005) Plant α-amylase: functions and role in carbohydrate metabolism. Biologia (Bratis) 60, 65-71.
    • (2005) Biologia (Bratis) , vol.60 , pp. 65-71
    • Stanley, D.1    Farnden, F.J.K.2    Macrae, A.E.3
  • 29
    • 45649084937 scopus 로고    scopus 로고
    • Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savinase reveal a novel mode of inhibition
    • Micheelsen PO, Vévodova J, De Maria L, Ostergaard PR, Friis EP, Wilson K Skjot M (2008) Structural and mutational analyses of the interaction between the barley alpha-amylase/subtilisin inhibitor and the subtilisin savinase reveal a novel mode of inhibition. J Mol Biol 380, 681-690.
    • (2008) J Mol Biol , vol.380 , pp. 681-690
    • Micheelsen, P.O.1    Vévodova, J.2    De Maria, L.3    Ostergaard, P.R.4    Friis, E.P.5    Wilson, K.6    Skjot, M.7
  • 30
    • 0346826288 scopus 로고    scopus 로고
    • Kinetics and energetics of the binding between barley alpha-amylase/subtilisin inhibitor and barley alpha-amylase 2 analyzed by surface plasmon resonance and isothermal titration calorimetry
    • Nielsen PK, Bønsager BC, Berland CR, Sigurskjold BW Svensson B (2003) Kinetics and energetics of the binding between barley alpha-amylase/subtilisin inhibitor and barley alpha-amylase 2 analyzed by surface plasmon resonance and isothermal titration calorimetry. Biochemistry 42, 1478-1487.
    • (2003) Biochemistry , vol.42 , pp. 1478-1487
    • Nielsen, P.K.1    Bønsager, B.C.2    Berland, C.R.3    Sigurskjold, B.W.4    Svensson, B.5
  • 32
    • 0001480645 scopus 로고
    • Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases
    • Legrand M, Kauffmann S, Geoffroy P Fritig B (1987) Biological function of pathogenesis-related proteins: four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci USA 84, 6750-6754.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6750-6754
    • Legrand, M.1    Kauffmann, S.2    Geoffroy, P.3    Fritig, B.4
  • 33
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate phenol-chloroform extraction
    • Chomczynski P Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate phenol-chloroform extraction. Anal Biochem 162, 156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 34
    • 0000369624 scopus 로고
    • A method for the determination of amino acid sequence in peptides
    • Edman P (1949) A method for the determination of amino acid sequence in peptides. Arch Biochem 22, 475.
    • (1949) Arch Biochem , vol.22 , pp. 475
    • Edman, P.1
  • 35
    • 33748037939 scopus 로고
    • Amylase alpha and beta
    • Bernfeld P (1955) Amylase alpha and beta. Methods Enzymol 1, 149-158.
    • (1955) Methods Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A Taplyakov A (1997) MOLREP: An automated program for molecular replacement. J Appl Crystallogr 30, 1022-1025.
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Taplyakov, A.2
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr Sect D: Biol Crystallogr 50, 760-763.
    • (1994) Acta Crystallogr Sect D: Biol Crystallogr , vol.50 , pp. 760-763
  • 40
    • 84889120137 scopus 로고
    • Improved methods for building models in electron density maps and the location of errors in these models
    • Jones TA, Zou J, Cowan SW Kjeldgaard M (1991) Improved methods for building models in electron density maps and the location of errors in these models. Acta Crystallogr A 47, 110-118.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-118
    • Jones, T.A.1    Zou, J.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.