Mycobacterium tuberculosis copper-regulated protein SocB is an intrinsically disordered protein that folds upon interaction with a synthetic phospholipid bilayer

ABSTRACT Multiple genes in Mycobacterium tuberculosis (Mtb) are regulated by copper including socAB (small orf induced by copper A and B), which is induced by copper and repressed by RicR (regulated in copper repressor). socA and socB encode hypothetical proteins of 61 and 54 amino acids, respective...

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Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2016-02, Vol.84 (2), p.193-200
Main Authors: Nowicka, Urszula, Hoffman, Morgan, Randles, Leah, Shi, Xiaoshan, Khavrutskii, Lyuba, Stefanisko, Karen, Tarasova, Nadya I., Darwin, K. Heran, Walters, Kylie J.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Copper - chemistry
Copper - metabolism
intrinsically disordered proteins
Intrinsically Disordered Proteins - chemistry
Intrinsically Disordered Proteins - metabolism
Lipid Bilayers - chemistry
Lipid Bilayers - metabolism
membrane protein
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Molecular Sequence Data
Mycobacterium tuberculosis
Mycobacterium tuberculosis (Mtb)
Mycobacterium tuberculosis - enzymology
SocB
synthetic phospholipid bilayer
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Summary:ABSTRACT Multiple genes in Mycobacterium tuberculosis (Mtb) are regulated by copper including socAB (small orf induced by copper A and B), which is induced by copper and repressed by RicR (regulated in copper repressor). socA and socB encode hypothetical proteins of 61 and 54 amino acids, respectively. Here, we use biophysical and computational methods to evaluate the SocB structure. We find that SocB lacks evidence for secondary structure, with no thermal cooperative unfolding event, according to circular dichroism measurements. 2D NMR spectra similarly exhibit hallmarks of a disordered structural state, which is also supported by analyzing SocB diffusion. Altogether, these findings suggest that by itself SocB is intrinsically disordered. Interestingly, SocB interacts with a synthetic phospholipid bilayer and becomes helical, which suggests that it may be membrane‐associated. Proteins 2016; 84:193–200. © 2015 Wiley Periodicals, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.24970