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Volumn 175, Issue 1, 2011, Pages 97-103

Crystal structure of the 30K protein from the silkworm Bombyx mori reveals a new member of the β-trefoil superfamily

Author keywords

Trefoil superfamily; 30K proteins; Crystal structure; Silkworm; Sugar binding site

Indexed keywords

BETA TREFOIL; BMLP7 PROTEIN; BOMBYX MORI LOW MOLECULAR WEIGHT LIPOPROTEIN; LIPOPROTEIN; SUGAR; TREFOIL PEPTIDE; UNCLASSIFIED DRUG; INSECT PROTEIN;

EID: 79956210260     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.04.003     Document Type: Article
Times cited : (28)

References (41)
  • 2
    • 0019162990 scopus 로고
    • Animal lipoproteins: chemistry, structure, and comparative aspects
    • Chapman M.J. Animal lipoproteins: chemistry, structure, and comparative aspects. J. Lipid Res. 1980, 21:789-853.
    • (1980) J. Lipid Res. , vol.21 , pp. 789-853
    • Chapman, M.J.1
  • 3
    • 33749340617 scopus 로고    scopus 로고
    • Enhancement of recombinant protein production in chinese hamster ovary cells through anti-apoptosis engineering using 30Kc6 gene
    • Choi S.S., Rhee W.J., Kim E.J., Park T.H. Enhancement of recombinant protein production in chinese hamster ovary cells through anti-apoptosis engineering using 30Kc6 gene. Biotechnol. Bioeng. 2006, 95:459-467.
    • (2006) Biotechnol. Bioeng. , vol.95 , pp. 459-467
    • Choi, S.S.1    Rhee, W.J.2    Kim, E.J.3    Park, T.H.4
  • 4
    • 0028103275 scopus 로고
    • Collaborative Computational Project
    • No. 4, The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-3.
    • Collaborative Computational Project, No. 4, 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-3.
    • (1994)
  • 5
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • DeLano Scientific LLC, Palo Alto, CA, USA.
    • DeLano, W.L., 2008. The PyMOL Molecular Graphics System. DeLano Scientific LLC, Palo Alto, CA, USA. http://www.pymol.org.
    • (2008)
    • DeLano, W.L.1
  • 7
    • 0036300580 scopus 로고    scopus 로고
    • Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module
    • Fujimoto Z., Kuno A., Kaneko S., Kobayashi H., Kusakabe I., et al. Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module. J. Mol. Biol. 2002, 316:65-78.
    • (2002) J. Mol. Biol. , vol.316 , pp. 65-78
    • Fujimoto, Z.1    Kuno, A.2    Kaneko, S.3    Kobayashi, H.4    Kusakabe, I.5
  • 8
    • 0009596477 scopus 로고
    • Low molecular weight lipoproteins in the haemolymph of the silkworm, Bombyx mori: Inheritance, isolation and some properties
    • Gamo T. Low molecular weight lipoproteins in the haemolymph of the silkworm, Bombyx mori: Inheritance, isolation and some properties. Insect Biochem. 1978, 8:457-470.
    • (1978) Insect Biochem. , vol.8 , pp. 457-470
    • Gamo, T.1
  • 9
    • 34248153179 scopus 로고    scopus 로고
    • Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope
    • Grahn E., Askarieh G., Holmner A., Tateno H., Winter H.C., et al. Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope. J. Mol. Biol. 2007, 369:710-721.
    • (2007) J. Mol. Biol. , vol.369 , pp. 710-721
    • Grahn, E.1    Askarieh, G.2    Holmner, A.3    Tateno, H.4    Winter, H.C.5
  • 10
    • 0030035805 scopus 로고    scopus 로고
    • The (QxW)3 domain: a flexible lectin scaffold
    • Hazes B. The (QxW)3 domain: a flexible lectin scaffold. Protein Sci. 1996, 5:1490-1501.
    • (1996) Protein Sci. , vol.5 , pp. 1490-1501
    • Hazes, B.1
  • 11
    • 0029034935 scopus 로고
    • A mosquitocidal toxin with a ricin-like cell-binding domain
    • Hazes B., Read R.J. A mosquitocidal toxin with a ricin-like cell-binding domain. Nat. Struct. Biol. 1995, 2:358-359.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 358-359
    • Hazes, B.1    Read, R.J.2
  • 12
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm L., Sander C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 1998, 26:316-319.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 13
    • 0034806263 scopus 로고    scopus 로고
    • Isolation and characterization of an apoptosis-inhibiting component from the hemolymph of Bombyx mori
    • Kim E.J., Rhee W.J., Park T.H. Isolation and characterization of an apoptosis-inhibiting component from the hemolymph of Bombyx mori. Biochem. Biophys. Res. Commun. 2001, 285:224-228.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 224-228
    • Kim, E.J.1    Rhee, W.J.2    Park, T.H.3
  • 14
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 15
    • 0031700043 scopus 로고    scopus 로고
    • Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins
    • Lerche M.H., Poulsen F.M. Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins. Protein Sci. 1998, 7:2490-2498.
    • (1998) Protein Sci. , vol.7 , pp. 2490-2498
    • Lerche, M.H.1    Poulsen, F.M.2
  • 16
    • 0037441653 scopus 로고    scopus 로고
    • Structure validation by Calpha geometry: phi, psi and Cbeta deviation
    • Lovell S.C., Davis I.W., Arendall W.B., de Bakker P.I., Word J.M., et al. Structure validation by Calpha geometry: phi, psi and Cbeta deviation. Proteins 2003, 50:437-450.
    • (2003) Proteins , vol.50 , pp. 437-450
    • Lovell, S.C.1    Davis, I.W.2    Arendall, W.B.3    de Bakker, P.I.4    Word, J.M.5
  • 17
    • 0031200975 scopus 로고    scopus 로고
    • Purification and characterization of a protease degrading 30 kDa yolk proteins of the silkworm, Bombyx mori
    • Maki N., Yamashita O. Purification and characterization of a protease degrading 30 kDa yolk proteins of the silkworm, Bombyx mori. Insect Biochem. Mol. Biol. 1997, 27:721-728.
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 721-728
    • Maki, N.1    Yamashita, O.2
  • 18
    • 20444471526 scopus 로고    scopus 로고
    • Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars
    • Mancheno J.M., Tateno H., Goldstein I.J., Martinez-Ripoll M., Hermoso J.A. Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars. J. Biol. Chem. 2005, 280:17251-17259.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17251-17259
    • Mancheno, J.M.1    Tateno, H.2    Goldstein, I.J.3    Martinez-Ripoll, M.4    Hermoso, J.A.5
  • 19
    • 65249181690 scopus 로고    scopus 로고
    • Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra
    • Maveyraud L., Niwa H., Guillet V., Svergun D.I., Konarev P.V., et al. Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra. Proteins 2009, 75:89-103.
    • (2009) Proteins , vol.75 , pp. 89-103
    • Maveyraud, L.1    Niwa, H.2    Guillet, V.3    Svergun, D.I.4    Konarev, P.V.5
  • 20
    • 3142615882 scopus 로고    scopus 로고
    • Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors
    • Meinhart A., Cramer P. Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors. Nature 2004, 430:223-226.
    • (2004) Nature , vol.430 , pp. 223-226
    • Meinhart, A.1    Cramer, P.2
  • 21
    • 0020772734 scopus 로고
    • Developmental and sex-dependent regulation of storage protein synthesis in the silkworm, Bombyx mori
    • Mine E., Izumi S., Katsuki M., Tomino S. Developmental and sex-dependent regulation of storage protein synthesis in the silkworm, Bombyx mori. Dev. Biol. 1983, 97:329-337.
    • (1983) Dev. Biol. , vol.97 , pp. 329-337
    • Mine, E.1    Izumi, S.2    Katsuki, M.3    Tomino, S.4
  • 22
    • 0026084931 scopus 로고
    • Structures and organization of major plasma protein genes of the silkworm Bombyx mori
    • Mori S., Izumi S., Tomino S. Structures and organization of major plasma protein genes of the silkworm Bombyx mori. J. Mol. Biol. 1991, 218:7-12.
    • (1991) J. Mol. Biol. , vol.218 , pp. 7-12
    • Mori, S.1    Izumi, S.2    Tomino, S.3
  • 24
    • 38649091349 scopus 로고    scopus 로고
    • Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin
    • Nakamura T., Tonozuka T., Ide A., Yuzawa T., Oguma K., et al. Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin. J. Mol. Biol. 2008, 376:854-867.
    • (2008) J. Mol. Biol. , vol.376 , pp. 854-867
    • Nakamura, T.1    Tonozuka, T.2    Ide, A.3    Yuzawa, T.4    Oguma, K.5
  • 25
    • 0037006986 scopus 로고    scopus 로고
    • High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding
    • Notenboom V., Boraston A.B., Williams S.J., Kilburn D.G., Rose D.R. High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding. Biochemistry 2002, 41:4246-4254.
    • (2002) Biochemistry , vol.41 , pp. 4246-4254
    • Notenboom, V.1    Boraston, A.B.2    Williams, S.J.3    Kilburn, D.G.4    Rose, D.R.5
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0030809260 scopus 로고    scopus 로고
    • WARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • Perrakis A., Sixma T.K., Wilson K.S., Lamzin V.S. WARP: improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models. Acta Crystallogr. D Biol. Crystallogr. 1997, 53:448-455.
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 28
    • 33847142225 scopus 로고    scopus 로고
    • CAVER: a new tool to explore routes from protein clefts, pockets and cavities
    • Petrek M., Otyepka M., Banas P., Kosinova P., Koca J., et al. CAVER: a new tool to explore routes from protein clefts, pockets and cavities. BMC Bioinf. 2006, 7:316.
    • (2006) BMC Bioinf. , vol.7 , pp. 316
    • Petrek, M.1    Otyepka, M.2    Banas, P.3    Kosinova, P.4    Koca, J.5
  • 30
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick G.M. A short history of SHELX. Acta Crystallogr. A 2008, 64:112-122.
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 31
    • 41849123860 scopus 로고    scopus 로고
    • Analysis of the structure and expression of the 30K protein genes in silkworm, Bombyx mori
    • Sun Q., Zhao P., Lin Y., Hou Y., Xia Q.Y., et al. Analysis of the structure and expression of the 30K protein genes in silkworm, Bombyx mori. Insect Sci. 2007, 14:5-14.
    • (2007) Insect Sci. , vol.14 , pp. 5-14
    • Sun, Q.1    Zhao, P.2    Lin, Y.3    Hou, Y.4    Xia, Q.Y.5
  • 32
    • 58549111415 scopus 로고    scopus 로고
    • Sugar-complex structures of the C-half domain of the galactose-binding lectin EW29 from the earthworm Lumbricus terrestris
    • Suzuki R., Kuno A., Hasegawa T., Hirabayashi J., Kasai K.I., et al. Sugar-complex structures of the C-half domain of the galactose-binding lectin EW29 from the earthworm Lumbricus terrestris. Acta Crystallogr. D Biol. Crystallogr. 2009, 65:49-57.
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 49-57
    • Suzuki, R.1    Kuno, A.2    Hasegawa, T.3    Hirabayashi, J.4    Kasai, K.I.5
  • 35
    • 33746403677 scopus 로고    scopus 로고
    • Silkworm midgut proteins interacting with a hemolymph protease inhibitor, CI-8
    • Ueno Y., He N., Ujita M., Yamamoto K., Banno Y., et al. Silkworm midgut proteins interacting with a hemolymph protease inhibitor, CI-8. Biosci. Biotechnol. Biochem. 2006, 70:1557-1563.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 1557-1563
    • Ueno, Y.1    He, N.2    Ujita, M.3    Yamamoto, K.4    Banno, Y.5
  • 36
    • 22444433560 scopus 로고    scopus 로고
    • Glucan-binding activity of silkworm 30-kDa apolipoprotein and its involvement in defense against fungal infection
    • Ujita M., Katsuno Y., Kawachi I., Ueno Y., Banno Y., et al. Glucan-binding activity of silkworm 30-kDa apolipoprotein and its involvement in defense against fungal infection. Biosci. Biotechnol. Biochem. 2005, 69:1178-1185.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 1178-1185
    • Ujita, M.1    Katsuno, Y.2    Kawachi, I.3    Ueno, Y.4    Banno, Y.5
  • 39
    • 10344265019 scopus 로고    scopus 로고
    • A draft sequence for the genome of the domesticated silkworm (Bombyx mori)
    • Xia Q., Zhou Z., Lu C., Cheng D., Dai F., et al. A draft sequence for the genome of the domesticated silkworm (Bombyx mori). Science 2004, 306:1937-1940.
    • (2004) Science , vol.306 , pp. 1937-1940
    • Xia, Q.1    Zhou, Z.2    Lu, C.3    Cheng, D.4    Dai, F.5


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