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PLoS One. 2015;10(11):e0142807
Authors: Maione V, Ruggiero A, Russo L, De Simone A, Pedone PV, Malgieri G, Berisio R, Isernia C
Abstract
Mycobacterium tuberculosis latent infection is maintained for years with no clinical symptoms and no adverse effects for the host. The mechanism through which dormant M. tuberculosis resuscitates and enters the cell cycle leading to tuberculosis is attracting much interest. The RPF family of proteins has been found to be responsible for bacteria resuscitation and normal proliferation. This family of proteins in M. tuberculosis is composed by five homologues (named RpfA-E) and understanding their conformational, structural and functional peculiarities is crucial to the design of therapeutic strategies.Therefore, we report the structural and dynamics characterization of the catalytic domain of RpfC from M. tubercolosis by combining Nuclear Magnetic Resonance, Circular Dichroism and Molecular Dynamics data. We also show how the formation of a disulfide bridge, highly conserved among the homologues, is likely to modulate the shape of the RpfC hydrophobic catalytic cleft. This might result in a protein function regulation via a "conformational editing" through a disulfide bond formation.
PMID: 26576056 [PubMed - as supplied by publisher]
[NMR paper] NMR conformational dynamics of an Anthrax Lethal Factor domain studied by multiple amino acid-selective labeling.
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Authors: Vourtsis DJ, Chasapis CT, Pairas G, Bentrop D, Spyroulias GA
Abstract
NMR-based structural biology urgently needs cost- and time-effective methods to assist both in the process of acquiring high-resolution NMR spectra and their subsequent...
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Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
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FEBS Lett. 2011 May 9;
Authors: Leineweber S, Schönig S, Seeger K
Type VII collagen as component of anchoring fibrils plays an important role in skin architecture, however, no detailed structural information is available. Here, we describe the recombinant expression, isotope labeling, and...
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[NMR paper] Three-dimensional modeling of the I-TevI homing endonuclease catalytic domain, a GIY-
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Protein Eng. 2001 Oct;14(10):717-21
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Using a recent version of the SICHO algorithm for in silico protein folding, we made a blind prediction of the tertiary...
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[NMR paper] Structure and dynamics of translation initiation factor aIF-1A from the archaeon Meth
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Translation initiation factor 1A (aIF-1A) from the archaeon Methanococcus jannaschii was expressed in Escherichia coli, purified, and characterized in terms of its structure and dynamics using...
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J Mol Biol. 2001 Aug 10;311(2):341-56
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The ligand-binding region of the low-density lipoprotein (LDL) receptor is formed by seven N-terminal, imperfect, cysteine-rich (LB)...
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[NMR paper] The NMR structure of the RNA binding domain of E. coli rho factor suggests possible R
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Nat Struct Biol. 1998 May;5(5):393-9
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NMR structure of the first extracellular domain of corticotropin releasing factor rec
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Biochemistry. 1994 Jul 19;33(28):8453-63
Authors: Zink T, Ross A, Lüers K, Cieslar C, Rudolph R, Holak TA
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NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain.
Linear Mode
