Crystallization of the oligopeptide-binding protein AppA from Bacillus subtilis.
نویسندگان
چکیده
AppA is the membrane-anchored extracellular receptor component of an ABC transporter responsible for the uptake of oligopeptides into Bacillus subtilis. AppA has been overexpressed as a cleavable maltose-binding protein fusion in Escherichia coli. Following removal of the fusion portion, AppA has been crystallized from morpholinoethanesulfonic acid-buffered solutions at pH 6.5 containing polyethylene glycol and zinc acetate. A complete X-ray diffraction data set extending to 2.3 A spacing has been collected.
منابع مشابه
Isolation and characterization of mutants of the Bacillus subtilis oligopeptide permease with altered specificity of oligopeptide transport.
Bacterial oligopeptide permeases are members of the large family of ATP binding cassette transporters and typically import peptides of 3 to 5 amino acids, apparently independently of sequence. Oligopeptide permeases are needed for bacteria to utilize peptides as nutrient sources and are sometimes involved in signal transduction pathways. The Bacillus subtilis oligopeptide permease stimulates co...
متن کاملStructural model and ligand interactions of the Xanthomonas axonopodis pv. citri oligopeptide-binding protein.
The oligopeptide-binding protein, OppA, ushers oligopeptide substrates to the membrane-associated oligopeptide permease (Opp), a multi-component ABC-type transporter involved in the uptake of oligopeptides by several bacterial species. In the present study, we report a structural model and an oligopeptide docking analysis of the OppA protein expressed by Xanthomonas axonopodis pv. citri (X. cit...
متن کاملCrystallographic analysis of Bacillus subtilis CsaA.
Bacillus subtilis CsaA (BsCsaA) has been proposed to act as a protein-secretion chaperone in the Sec-dependent translocation pathway, possibly compensating for the lack of SecB in the Gram-positive eubacterium Bacillus subtilis. This paper presents the cloning, purification, crystallization and structures of BsCsaA in two space groups (P42(1)2 and P3(2)21) solved and refined to resolutions of 1...
متن کاملAnti-TRAP protein from Bacillus subtilis: crystallization and internal symmetry.
Anti-TRAP protein regulates the expression of tryptophan biosynthetic genes by binding to TRAP and preventing formation of the TRAP-RNA complex. Anti-TRAP from Bacillus subtilis has been crystallized by vapour diffusion. The crystals belong to space group P1, with unit-cell parameters a = 51.6, b = 60.1, c = 60.4 A, alpha = 114.0, beta = 101.4, gamma = 100.5 degrees. X-ray data have been collec...
متن کاملBacillus subtilis as a Host for Recombinant Hemagglutinin Production of the Influenza A (H5N1) Virus
Abstract Background and Aims: Influenza A(H5N1) viruses circulating in animals might evolve and acquire the ability to spread from human to human and thus start a pandemic. Hemagglutinin (HA) has been shown to play a major role in binding of influenza virus to its target cell and the main neutralizing antibody responses elicit against this region. Recent studies have shown that...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Acta crystallographica. Section D, Biological crystallography
دوره 60 Pt 1 شماره
صفحات -
تاریخ انتشار 2004