Crystal structure of the bacterial protein export chaperone SecB

Nature Structural Biology

Volumn 7, Issue 12, 2000, Pages 1172-1177

  Xu, Z ^a   Knafels, J D ^a   Yoshino, K ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; CHAPERONE; DIMER; POLYPEPTIDE; PROTEIN SECB; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; CRYSTAL STRUCTURE; HAEMOPHILUS INFLUENZAE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CARRIER PROTEINS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI PROTEINS; HAEMOPHILUS INFLUENZAE; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PEPTIDES; PLIABILITY; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); HAEMOPHILUS INFLUENZAE;

EID: 0033675260     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/82040     Document Type: Article

References (36)

1. The signal peptide
2. Two cellular components, PrlA and SecB, that recognize different sequence determinants are required for efficient protein export
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4. Escherichia coli SecB protein associates with exported protein precursors in vivo
5. Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins
6. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
7. Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA
8. Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export
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10. Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro
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14. Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo
15. A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB
16. Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB
17. Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers
18. Thermodynamics of substrate binding to the chaperone SecB
19. No specific recognition of leader peptide by SecB, a chaperone involved in protein export
20. Calorimetric analyses of the interaction between SecB and its ligands
21. Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor
22. PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine
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32. Improved methods for binding protein models in electron density maps and the location of errors in these models
33. CLUSTAL W: Improving the sensitivity of progressive multiple squence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
34. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
35. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons