Mycobacterium tuberculosis ArfA Rv0899: Difference between revisions
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' size='350' frame='true' align='right' caption='NMR structure of uncharacterized protein Rv0899 (PDB code [[2l26]])' scene='Insert optional scene name here' /> | ' size='350' frame='true' align='right' caption='NMR structure of uncharacterized protein Rv0899 (PDB code [[2l26]])' scene='Insert optional scene name here' /> | ||
== Function == | == Function == | ||
Protein Rv0899 from '''''Mycobacterium tuberculosis''''' [http://he.wikipedia.org/wiki/Mycobacterium_tuberculosis] belongs to the OmpA (outer membrane protein A) family of outer membrane proteins.The deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. It was proposed that Rv0899 forms an oligomeric channel to carry out such functions.Using [[NMR]] chemical shift perturbation and isothermal calorimetric titration assays, Rv0899 was able to interact with Zn(2+) ions, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition. | Protein Rv0899 from '''''Mycobacterium tuberculosis''''' [http://he.wikipedia.org/wiki/Mycobacterium_tuberculosis] belongs to the OmpA (outer membrane protein A) family of outer membrane proteins.The deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. It was proposed that Rv0899 forms an oligomeric channel to carry out such functions.Using [[NMR]] chemical shift perturbation and [[isothermal calorimetric titration assays]], Rv0899 was able to interact with Zn(2+) ions, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition. | ||
<ref>PMID: 22108166 </ref> | <ref>PMID: 22108166 </ref> | ||
Rv0899 has been proposed to act as an outer membrane [[porin]] and to contribute to the bacterium's adaptation to the acidic environment of the phagosome during infection. The gene is restricted to pathogenic mycobacteria and, thus, is an attractive candidate for the development of anti-tuberculosis chemotherapy. The 326-residue protein contains three domains: an N-terminal domain (residues 1-72) that includes a sequence of 20 hydrophobic amino acids required for membrane translocation, a central B domain (residues 73-200) with homology to the conserved putative lipid-binding BON (bacterial OsmY and nodulation) superfamily, and a C domain (residues 201-326) with homology to the OmpA-C-like superfamily of periplasmic peptidoglycan-binding sequences, found in several types of bacterial membrane proteins, including in the C-terminus of the Escherichia coli outer membrane protein OmpA. Rv0899 does not form a transmembrane beta-barrel. Residues 73-326 form a mixed alpha/beta-globular structure, encompassing two independently folded modules corresponding to the B and C domains connected by a flexible linker. The B domain folds with three parallel/antiparallel alpha-helices packed against six parallel/antiparallel beta-strands that form a flat beta-sheet. The core is hydrophobic, while the exterior is polar and predominantly acidic.<ref>PMID: 20199110</ref> | Rv0899 has been proposed to act as an outer membrane [[porin]] and to contribute to the bacterium's adaptation to the acidic environment of the phagosome during infection. The gene is restricted to pathogenic mycobacteria and, thus, is an attractive candidate for the development of anti-tuberculosis chemotherapy. The 326-residue protein contains three domains: an N-terminal domain (residues 1-72) that includes a sequence of 20 hydrophobic amino acids required for membrane translocation, a central B domain (residues 73-200) with homology to the conserved putative lipid-binding BON (bacterial OsmY and nodulation) superfamily, and a C domain (residues 201-326) with homology to the OmpA-C-like superfamily of periplasmic peptidoglycan-binding sequences, found in several types of bacterial membrane proteins, including in the C-terminus of the Escherichia coli outer membrane protein OmpA. Rv0899 does not form a transmembrane beta-barrel. Residues 73-326 form a mixed alpha/beta-globular structure, encompassing two independently folded modules corresponding to the B and C domains connected by a flexible linker. The B domain folds with three parallel/antiparallel alpha-helices packed against six parallel/antiparallel beta-strands that form a flat beta-sheet. The core is hydrophobic, while the exterior is polar and predominantly acidic.<ref>PMID: 20199110</ref> | ||