2FWV

Crystal Structure of Rv0813

Summary for 2FWV

• Entry DOI: 10.2210/pdb2fwv/pdb
• Descriptor: hypothetical protein MtubF_01000852, 1,4-DIETHYLENE DIOXIDE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: structural genomics, conserved hypothetical, unknown function, restricted to actinomycetes, fatty acid binding protein like, structural proteomics in europe, spine
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 24369.87

Authors

Shepard, W.,Haouz, A.,Grana, M.,Buschiazzo, A.,Betton, J.M.,Cole, S.T.,Alzari, P.M.,Structural Proteomics in Europe (SPINE) (deposition date: 2006-02-03, release date: 2006-08-03, Last modification date: 2024-03-13)

Primary citation

Shepard, W.,Haouz, A.,Grana, M.,Buschiazzo, A.,Betton, J.M.,Cole, S.T.,Alzari, P.M.
The Crystal Structure of Rv0813c from Mycobacterium tuberculosis Reveals a New Family of Fatty Acid-Binding Protein-Like Proteins in Bacteria
J.Bacteriol., 189:1899-1904, 2007

PubMed Abstract: 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 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.

PubMed: 17172346
DOI: 10.1128/JB.01435-06

Experimental method

X-RAY DIFFRACTION (1.7 Å)