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J. Bacteriol. doi:10.1128/JB.01435-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of FABP-like proteins in bacteria

Unité de Biochimie Structurale & CNRS URA2185, 25 rue du Docteur Roux, 75724 Paris, France; Synchrotron Soleil, L'Orme des Merisiers, Saint Aubin, BP 48, 91192 Gif-sur-Yvette, France; Plate-forme de cristallogenèse et Diffraction des Rayons X, 25 rue du Docteur Roux, 75724 Paris, France; and Unité de Génétique Moléculaire Bactérienne, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris, France

^* To whom correspondence should be addressed. Email: alzari{at}pasteur.fr.

	Abstract

The gene Rv0813c from Mycobacterium tuberculosis, which codes for a hypothetical protein of unknown function, is conserved within the actinomycetales order but absent elsewhere. The crystal structure of Rv0813c reveals a new family of proteins that resemble the fatty acid-binding proteins (FABPs) found in eukaryotes. Rv0813c adopts the 10-stranded -barrel fold typical of FABPs, but lacks the double-helix insert that covers the entry to the binding site in the eukaryotic proteins. The barrel encloses a deep cavity, at the bottom of which a small cyclic ligand was found to bind to the hydroxyl group of Tyr192. This residue is part of a conserved Arg-X-Tyr motif much like the triad that binds the carboxylate group of fatty acids in FABPs. Most of the residues forming the internal surface of the cavity are conserved in homologous protein sequences found in CG-rich prokaryotes, strongly suggesting that Rv0813c is member of a new family of bacterial FABP-like proteins, which may have a role in the recognition, transport and/or storage of small molecules in the bacterial cytosol.

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