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Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Eschericha coli (1996)

Jia, J. ; Lindqvist, Y. ; Schneider, G. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 52 (1996), S. 192-193

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: Recombinant transaldolase from Escherichia coli, an enzyme of the pentose phosphate pathway has been crystallized by the vapor-diffusion method using polyethylene glycol 6000 as precipitant. The crystals are orthorhombic, space group P212121 with cell dimensions a = 68.9, b = 91.3 and c = 130.5 Å and diffract to 2 Å resolution on a conventional X-ray source. The asymmetric unit very likely contains two subunits, corresponding to a packing density of 2.9 Å3 Da−1.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444995010365

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Export of the periplasmic NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis (1996)

Wiegert, Thomas ; Sahm, Hermann ; Sprenger, G. A.

Springer

Archives of microbiology 166 (1996), S. 32-41

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ISSN: 1432-072X

Keywords: Key words Glucose-fructose oxidoreductase ; Zymomonas mobilis ; Gfo-deficient mutant ; Sorbitol ; Protein export ; Signal sequence ; Periplasmic NADP

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Glucose-fructose oxidoreductase (GFOR) of the gram-negative bacterium Zymomonas mobilis is a periplasmic enzyme with the tightly bound cofactor NADP. The preprotein carries an unusually long N-terminal signal sequence of 52 amino acid residues. A sorbitol-negative mutant strain (ACM3963) was found to be deficient in GFOR activity and was used for the expression of plasmid-borne copies of the wild-type gfo gene or of alleles encoding alterations in the signal sequence of the pre-GFOR protein. Z. mobilis cells with the wild-type gfo allele translocated pre-GFOR, at least partially, via the Sec pathway since CCCP (carboxylcyanide-m-chlorophenylhydrazone; uncoupler of proton motive force) or sodium azide (inhibitor of SecA) abolished the processing of GFOR. A gfo allele with the hydrophobic region of the signal sequence removed (residues 32–46; Δ32–46) led to a protein that was no longer processed, but showed full enzymatic activity (180 U/mg) and had the cofactor NADP firmly bound. A deletion in the n-region of the signal sequence (residues 2–20; Δ2–20) or exchange of the entire GFOR signal sequence with the signal sequence of gluconolactonase of Z. mobilis led to active and processed GFOR. Strain ACM3963 could not grow in the presence of high sugar concentrations (1 M sucrose) unless sorbitol was added. The presence of the plasmid-borne gfo wild-type allele or of the Δ2–20 deletion led to the restoration of growth on media with 1 M sucrose, whereas the presence of the Δ32–46 deletion led to a growth behavior similar to that of strain ACM3963, with no sorbitol formation from sucrose.