Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI

Niemann H, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW (2006)
J Mol Biol 356(1): 1-8.

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Department
Fakultät für Chemie > Biochemie IV
Keywords
Crystallography ; X-Ray ; Disulfides/*chemistry/metabolism ; Tertiary ; Histidine/genetics/metabolism ; Momordica/*chemistry/genetics ; Molecular Sequence Data ; Molecular ; Models ; Nuclear Magnetic Resonance ; Biomolecular ; Plant Proteins/*chemistry/genetics/*metabolism ; Protein Structure ; Recombinant Fusion Proteins/chemistry/genetics/metabolism ; Ribonucleases/genetics/*metabolism ; Sequence Alignment ; Amino Acid Sequence
Publishing Year
2006
ISSN
0022-2836
PUB-ID

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Niemann H, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW. Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol. 2006;356(1):1-8.
Niemann, H., Schmoldt, H. U., Wentzel, A., Kolmar, H., & Heinz, D. W. (2006). Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol, 356(1), 1-8. doi:10.1016/j.jmb.2005.11.005
Niemann, H., Schmoldt, H. U., Wentzel, A., Kolmar, H., and Heinz, D. W. (2006). Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol 356, 1-8.
Niemann, H., et al., 2006. Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol, 356(1), p 1-8.
H. Niemann, et al., “Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI”, J Mol Biol, vol. 356, 2006, pp. 1-8.
Niemann, H., Schmoldt, H.U., Wentzel, A., Kolmar, H., Heinz, D.W.: Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol. 356, 1-8 (2006).
Niemann, Hartmut, Schmoldt, H. U., Wentzel, A., Kolmar, H., and Heinz, D. W. “Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI”. J Mol Biol 356.1 (2006): 1-8.
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9 Citations in Europe PMC

Data provided by Europe PubMed Central.

Cellular disulfide bond formation in bioactive peptides and proteins.
Patil NA, Tailhades J, Hughes RA, Separovic F, Wade JD, Hossain MA., Int J Mol Sci 16(1), 2015
PMID: 25594871
PredSTP: a highly accurate SVM based model to predict sequential cystine stabilized peptides.
Islam SM, Sajed T, Kearney CM, Baker EJ., BMC Bioinformatics 16(), 2015
PMID: 26142484
Barnase and binase: twins with distinct fates.
Ulyanova V, Vershinina V, Ilinskaya O., FEBS J 278(19), 2011
PMID: 21824291
Engineered cystine knot miniproteins as potent inhibitors of human mast cell tryptase beta.
Sommerhoff CP, Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Diederichsen U, Kolmar H., J Mol Biol 395(1), 2010
PMID: 19852971
Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.
de Marco A., Microb Cell Fact 8(), 2009
PMID: 19442264
Head-to-tail cyclized cystine-knot peptides by a combined recombinant and chemical route of synthesis.
Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Wentzel A, Frauendorf H, Sommerhoff CP, Diederichsen U, Kolmar H., Chembiochem 9(1), 2008
PMID: 18058774
Chemical and biomimetic total syntheses of natural and engineered MCoTI cyclotides.
Thongyoo P, Roqué-Rosell N, Leatherbarrow RJ, Tate EW., Org Biomol Chem 6(8), 2008
PMID: 18385853
Evaluation and improvement of the properties of the novel cystine-knot microprotein McoEeTI for oral administration.
Werle M, Kafedjiiski K, Kolmar H, Bernkop-Schnürch A., Int J Pharm 332(1-2), 2007
PMID: 17070661
Eukaryotic integral membrane protein expression utilizing the Escherichia coli glycerol-conducting channel protein (GlpF).
Neophytou I, Harvey R, Lawrence J, Marsh P, Panaretou B, Barlow D., Appl Microbiol Biotechnol 77(2), 2007
PMID: 17828601

42 References

Data provided by Europe PubMed Central.

Structural analysis of regulatory protein domains using GST-fusion proteins.
Zhan Y, Song X, Zhou GW., Gene 281(1-2), 2001
PMID: 11750122
Crystal structures of fusion proteins with large-affinity tags.
Smyth DR, Mrozkiewicz MK, McGrath WJ, Listwan P, Kobe B., Protein Sci. 12(7), 2003
PMID: 12824478
Crystal structure of a dominant B-cell epitope from the preS2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein.
Saul FA, Vulliez-le Normand B, Lema F, Bentley GA., J. Mol. Biol. 280(2), 1998
PMID: 9654443
Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins.
Kobe B, Center RJ, Kemp BE, Poumbourios P., Proc. Natl. Acad. Sci. U.S.A. 96(8), 1999
PMID: 10200260
Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera.
Ke A, Wolberger C., Protein Sci. 12(2), 2003
PMID: 12538894
Crystal structure of the SarR protein from Staphylococcus aureus.
Liu Y, Manna A, Li R, Martin WE, Murphy RC, Cheung AL, Zhang G., Proc. Natl. Acad. Sci. U.S.A. 98(12), 2001
PMID: 11381122
Crystallization and preliminary X-ray diffraction analysis of the extracellular domain of the cell surface antigen CD38 complexed with ganglioside
Kukimoto, J. Biochem. (Tokyo) 127(), 2000
A C-terminal segment of the V1R vasopressin receptor is unstructured in the crystal structure of its chimera with the maltose-binding protein
Adikesavan, Acta Crystallog. sect. F 61(), 2005
Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.
Niemann HH, Knetsch ML, Scherer A, Manstein DJ, Kull FJ., EMBO J. 20(21), 2001
PMID: 11689422
The KNOTTIN website and database: a new information system dedicated to the knottin scaffold
Gelly, Nucl. Acids Res. 32(), 2004
Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
Kabsch, J. Appl. Crystallog. 26(), 1993
Rapid automated molecular replacement by evolutionary search
Kissinger, Acta Crystallog. sect. D 55(), 1999
Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals.
Kantardjieff KA, Rupp B., Protein Sci. 12(9), 2003
PMID: 12930986
Improved methods for building protein models in electron density maps and the location of errors in these models
Jones, Acta Crystallog. sect. A 2(), 1991
Macromolecular TLS refinement in REFMAC at moderate resolutions.
Winn MD, Murshudov GN, Papiz MZ., Meth. Enzymol. 374(), 2003
PMID: 14696379
ARP/wARP and molecular replacement
Perrakis, Acta Crystallog. sect. D 57(), 2001
Improved R-factors for diffraction data analysis in macromolecular crystallography
Diederichs, Nature Struct. Biol. 4(), 1997

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