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Front cover illustration: Structural model of the homotetrameric form of MabA (FabG1) from Mycobacterium tuberculosis, complexed with its coenzyme, NADPH. MabA is an alpha-ketoacyl reductase involved in long-chain fatty acid elongation and is part of a large multi-enzyme complex called FAS-II. Traces of the four subunits are displayed as ribbons in four different colours. The nicotinamide portion of NADPH (yellow sticks) points into the substrate-binding pocket. Amino acid residues involved in this pocket are shown: hydrophobic residues are green and orange, the catalytic triad is red and polar residues surrounding the triad are white. The unique Trp residue (yellow) allowed monitoring of ligand binding by fluorescence spectroscopy. Courtesy Gilles Labesse, CBS-INSERM-CNRS, Montpellier, and Annaïk Quémard, IPBS-CNRS, Université Paul Sabatier, Toulouse, France. See the paper by Marrakchi et al. on pp. 951-960.