2a7y
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Solution Structure of the Conserved Hypothetical Protein Rv2302 from the Bacterium Mycobacterium tuberculosis
OverviewOverview
The Mycobacterium tuberculosis protein Rv2302 (80 residues; molecular mass, of 8.6 kDa) has been characterized using nuclear magnetic resonance (NMR), and circular dichroism (CD) spectroscopy. While the biochemical function, of Rv2302 is still unknown, recent microarray analyses show that Rv2302 is, upregulated in response to starvation and overexpression of heat shock, proteins and, consequently, may play a role in the biochemical processes, associated with these events. Rv2302 is a monomer in solution as shown by, size exclusion chromatography and NMR spectroscopy. CD spectroscopy, suggests that Rv2302 partially unfolds upon heating and that this, unfolding is reversible. Using NMR-based methods, the solution structure, of Rv2302 was determined. The protein contains a five-strand, antiparallel, beta-sheet core with one C-terminal alpha-helix (A61 to A75) nestled, against its side. Hydrophobic interactions between residues in the, alpha-helix and beta-strands 3 and 4 hold the alpha-helix near the, beta-sheet core. The electrostatic potential on the solvent-accessible, surface is primarily negative with the exception of a positive arginine, pocket composed of residues R18, R70, and R74. Steady-state {(1)H}-(15)N, heteronuclear nuclear Overhauser effects indicate that the protein's core, is rigid on the picosecond timescale. The absence of amide cross-peaks for, residues G13 to H19 in the (1)H-(15)N heteronuclear single quantum, correlation spectrum suggests that this region, a loop between, beta-strands 1 and 2, undergoes motion on the millisecond to microsecond, timescale. Dali searches using the structure closest to the average, structure do not identify any high similarities to any other known protein, structure, suggesting that the structure of Rv2302 may represent a novel, protein fold.
About this StructureAbout this Structure
2A7Y is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the conserved hypothetical protein Rv2302 from Mycobacterium tuberculosis., Buchko GW, Kim CY, Terwilliger TC, Kennedy MA, J Bacteriol. 2006 Aug;188(16):5993-6001. PMID:16885468
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