000151208 001__ 151208
000151208 005__ 20181203021957.0
000151208 022__ $$a0021-9193
000151208 02470 $$2PMID$$a17172346
000151208 0247_ $$2doi$$a10.1128/JB.01435-06
000151208 037__ $$aARTICLE
000151208 245__ $$aThe crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of fatty acid-binding protein-like proteins in bacteria
000151208 269__ $$a2006
000151208 260__ $$c2006
000151208 336__ $$aJournal Articles
000151208 520__ $$aThe gene Rv0813c from Mycobacterium tuberculosis, which codes for a hypothetical protein of unknown function, is conserved within the order Actinomycetales but absent elsewhere. The crystal structure of Rv0813c reveals a new family of proteins that resemble the fatty acid-binding proteins (FABPs) found in eukaryotes. Rv0813c adopts the 10-stranded beta-barrel fold typical of FABPs but lacks the double-helix insert that covers the entry to the binding site in the eukaryotic proteins. The barrel encloses a deep cavity, at the bottom of which a small cyclic ligand was found to bind to the hydroxyl group of Tyr192. This residue is part of a conserved Arg-X-Tyr motif much like the triad that binds the carboxylate group of fatty acids in FABPs. Most of the residues forming the internal surface of the cavity are conserved in homologous protein sequences found in CG-rich prokaryotes, strongly suggesting that Rv0813c is a member of a new family of bacterial FABP-like proteins that may have roles in the recognition, transport, and/or storage of small molecules in the bacterial cytosol.
000151208 700__ $$aShepard, William
000151208 700__ $$aHaouz, Ahmed
000151208 700__ $$aGraña, Martin
000151208 700__ $$aBuschiazzo, Alejandro
000151208 700__ $$aBetton, Jean-Michel
000151208 700__ $$0243892$$g177247$$aCole, Stewart T
000151208 700__ $$aAlzari, Pedro M
000151208 773__ $$j189$$tJournal of bacteriology$$k5$$q1899-904
000151208 909C0 $$xU11742$$0252302$$pUPCOL
000151208 909CO $$pSV$$particle$$ooai:infoscience.tind.io:151208
000151208 937__ $$aEPFL-ARTICLE-151208
000151208 973__ $$rREVIEWED$$sPUBLISHED$$aEPFL
000151208 980__ $$aARTICLE