DOI: 10.1016/j.jsb.2003.09.012. Crystal structure of SecB from Escherichia coli

Crystal structure of SecB from Escherichia coli

10.1016/j.jsb.2003.09.012

Crossref journal-article

Elsevier BV

Journal of Structural Biology (78)

Bibliography

Dekker, C., Kruijff, B. de, & Gros, P. (2003). Crystal structure of SecB from Escherichia coli. Journal of Structural Biology, 144(3), 313â319.

Authors 3

Carien Dekker (first)
Ben de Kruijff (additional)
Piet Gros (additional)

References 31 Referenced 56

10.1074/jbc.270.14.7902 / J. Biol. Chem. / The C terminus of SecA is involved in both lipid binding and SecB binding by Breukink (1995)
10.1107/S0907444998003254 / Acta Crystallogr. D / Crystallography & NMR system: a new software suite for macromolecular structure determination by Brunger (1998)
CCP4. 1994. Collaborative Computational Project No. 4: The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760–763 (10.1107/S0907444994003112)
10.1006/jsbi.1999.4179 / J. Struct. Biol. / Crystals of acetylated SecB diffract to 2.3-Å resolution by Dekker (1999)
10.1042/bst0230981 / Biochem. Soc. Trans. / SecA, a novel ATPase that converts chemical energy into a mechanical force to drive precursor protein translocation by Driessen (1995)
10.1038/88549 / Nat. Struct. Biol. / The structural basis of protein targeting and translocation in bacteria by Driessen (2001)
10.1046/j.1365-2958.1998.00997.x / Mol. Microbiol. / Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA by Fekkes (1998)
10.1093/emboj/16.20.6105 / EMBO J. / The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation by Fekkes (1997)
10.1016/0092-8674(90)90160-G / Cell / The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane by Hartl (1990)
10.1126/science.1074424 / Science / Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA by Hunt (2002)
10.1107/S0108767390010224 / Acta Crystallogr. A / Improved methods for building protein models in electron density maps and the location of errors in these models by Jones (1991)
10.1074/jbc.270.43.25920 / J. Biol. Chem. / Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein by Khisty (1995)
10.1074/jbc.270.39.22831 / J. Biol. Chem. / Diverse effect of mutation on the activity of the Escherichia coli export chaperone SecB by Kimsey (1995)
10.1074/jbc.274.48.34219 / J. Biol. Chem. / Substrate specificity of the SecB chaperone by Knoblauch (1999)
10.1107/S0021889891004399 / J. Appl. Crystallogr. / MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures by Kraulis (1991)
10.1007/BF00763171 / J. Bioenerg. Biomem. / SecB protein: a cytosolic export factor that associates with nascent exported proteins by Kumamoto (1990)
10.1074/jbc.274.27.19397 / J. Biol. Chem. / Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers by Muren (1999)
10.1107/S0108767393007597 / Acta Crystallogr. A / AMoRe: an automated package for molecular replacement by Navaza (1994)
10.1002/prot.340110407 / Proteins: Struct. Funct. Genet. / Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons by Nicholls (1991)
10.1016/S0076-6879(97)76066-X / Methods Enzymol. / Processing of X-ray diffraction data collected in oscillation mode by Otwinowski (1997)
10.1074/jbc.275.25.18698 / J. Biol. Chem. / A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone SecB by Panse (2000)
10.1126/science.1631545 / Science / Peptide binding by chaperone SecB: implications for recognition of nonnative structure by Randall (1992)
10.1002/pro.5560071115 / Protein Sci. / The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding by Randall (1998)
10.1038/81907 / Nat. Struct. Biol. / The promiscuous and specific sides of SecB by Randall (2000)
10.1007/PL00012488 / Cell. Mol. Life Sci. / SecB, one small chaperone in the complex milieu of the cell by Randall (2002)
{'key': '10.1016/j.jsb.2003.09.012_BIB26', 'first-page': '65', 'article-title': 'High selectivity with low specificity: how SecB has solved the paradox of chaperone binding', 'volume': '20', 'author': 'Randall', 'year': '1995', 'journal-title': 'TIBS'} / TIBS / High selectivity with low specificity: how SecB has solved the paradox of chaperone binding by Randall (1995)
10.1074/jbc.272.31.19314 / J. Biol. Chem. / Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands by Topping (1997)
10.1002/pro.5560030502 / Protein Sci. / Determination of the binding frame within a physiological ligand for the chaperone SecB by Topping (1994)
10.1074/jbc.M009584200 / J. Biol. Chem. / Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium by Topping (2001)
10.1006/bbrc.1999.1590 / Biochem. Biophys. Res. Commun. / A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB by Volkert (1999)
10.1038/82040 / Nat. Struct. Biol. / Crystal structure of the bacterial protein export chaperone SecB by Xu (2000)

Dates

Type	When
Created	21 years, 10 months ago (Oct. 22, 2003, 8:20 a.m.)
Deposited	6 years, 6 months ago (Feb. 19, 2019, 4:23 a.m.)
Indexed	3 months, 2 weeks ago (May 16, 2025, 8:44 a.m.)
Issued	21 years, 9 months ago (Dec. 1, 2003)
Published	21 years, 9 months ago (Dec. 1, 2003)
Published Print	21 years, 9 months ago (Dec. 1, 2003)

Funders 0

None

BibTeX

@article{Dekker_2003, title={Crystal structure of SecB from Escherichia coli}, volume={144}, ISSN={1047-8477}, url={http://dx.doi.org/10.1016/j.jsb.2003.09.012}, DOI={10.1016/j.jsb.2003.09.012}, number={3}, journal={Journal of Structural Biology}, publisher={Elsevier BV}, author={Dekker, Carien and Kruijff, Ben de and Gros, Piet}, year={2003}, month=dec, pages={313–319} }

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