By Alton Meister
Site visitors ATPases: A Superfamily of delivery Proteins working from Escherichia coli to people (G. Ames, et al.).
The respiration Burst Oxidase (B. Babior).
seasoned- and Antioxidant capabilities of Quinones and Quinone Reductase in Mammalian Cells (E. Cadenas & P. Hochstein).
The Redox facilities of Ribonucleotide Reductase of Escherichia coli (M. Fontecave, et al.).
lengthy diversity Intramolecular associated features within the Calcium shipping ATPase (G. Inesi, et al.).
Hydrogen-Bonding in Carbohydrates and Hydrate Inclusion Compounds (G. Jeffrey).
Methylation of mRNA (P. Narayan & F. Rottman).
Mammalian Nitric Oxide Synthases (D. Stuehr & O. Griffith).
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Extra resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 65
1986); MDRPF(N) and MDRPF(C), N-terminal and C-terminal domains. , 1989; McGrath and Varshavsky, 1989); WHITE, gene product of the whire gene of U . The < o r > carats following the names indicate that the sequence continues beyond the N- or C-terminal residues in the alignment. hisf mutations are noted above the alignment and are discussed in the text. Residues modified by 8-azido ATP are denoted with an 8. Positions corresponding to cystic fibrosis mutations are marked with arrowheads. GIOVANNA AMES ET AL.
Accessibility of the transporter at the inner or outer surface is hypothesized to be mediated through a series of conformational changes. 36 GIOVANNA AMES ET AL. vergent evolution from a common ancestral carrier. Among the other essential and common functions, a likely possibility is the signal transmission from the substrate-occupied site(s) to the energy-transducing triggering mechanism, or vice versa. In this scenario the substrate-binding site could be located either on the conserved component, accounting for the nonconserved regions, or on the hydrophobic component(s).
1991). Structure-function analysis of the histidine permease and comparison with cystic fibrosis. J . B i d C h e ~266, . 18714-18719. Speiser, D. M. and Ames, G. -L. (1991). Mutants of the histidine periplasmic permease of Salrnonel/u tvphimuvirtrn that allow transport in the absence of histidinebinding proteins, J . , 173, 1444-1451. Treptow, N. A. and Shuman, H. A. (1985). Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichiu c,o/i maltose transport system, J .