This Article Full Text Full Text (PDF) Other Versions of this Article: JB.01435-06v1 189/5/1899    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Shepard, W. Articles by Alzari, P. M. Search for Related Content PubMed PubMed Citation Articles by Shepard, W. Articles by Alzari, P. M.

The Crystal Structure of Rv0813c from Mycobacterium tuberculosis Reveals a New Family of Fatty Acid-Binding Protein-Like Proteins in Bacteria

Unité de Biochimie Structurale and CNRS URA 2185, 25 rue du Docteur Roux, 75724 Paris, France,¹ Synchrotron Soleil, L'Orme des Merisiers, Saint Aubin, BP 48, 91192 Gif-sur-Yvette, France,² Plate-forme de Cristallogenèse et Diffraction des Rayons X, 25 rue du Docteur Roux, 75724 Paris, France,³ Unité de Génétique Moléculaire Bactérienne, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris, France⁴

Received 10 September 2006/ Accepted 5 December 2006

The gene Rv0813c from Mycobacterium tuberculosis, which codes for a hypothetical protein of unknown function, is conserved within the order Actinomycetales 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 ß-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 a member of a new family of bacterial FABP-like proteins that may have roles in the recognition, transport, and/or storage of small molecules in the bacterial cytosol.

Published ahead of print on 15 December 2006.

This article has been cited by other articles:

• Grana, M., Haouz, A., Buschiazzo, A., Miras, I., Wehenkel, A., Bondet, V., Shepard, W., Schaeffer, F., Cole, S. T., Alzari, P. M. (2007). The crystal structure of M. leprae ML2640c defines a large family of putative S-adenosylmethionine-dependent methyltransferases in mycobacteria. Protein Sci. 16: 1896-1904 [Abstract] [Full Text]