Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

Bent, Colin J.; Isaacs, Neil W.; Mitchell, Tim; Riboldi-Tunnicliffe, A.

doi:10.1107/s090744490300372x

Cited by 3 publications

(3 citation statements)

References 5 publications

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“…These β-turn assignments would explain the absence of similar positive bands in the range ∼1260−1295 cm -1 and negative bands in the range ∼1340−1380 cm -1 in the ROA spectrum of subtilisin Carlsberg since the parallel sheet in this protein is based on the β−α−β motif 30 in which the parallel strands are connected by α-helix loops. These bands are absent in the ROA spectra of other proteins we have studied having parallel β-sheet based on the β−α−β motif, including aldolase 18 and the receiver domain from MicA (unpublished), a response regulator from Streptococcus pneumoniae …”

Section: Resultsmentioning

confidence: 98%

A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(l-lysine) to the Prion Protein

et al. 2003

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The vibrational Raman optical activity (ROA) spectrum of a polypeptide in a model beta-sheet conformation, that of poly(l-lysine), was measured for the first time, and the alpha-helix --> beta-sheet transition monitored as a function of temperature in H(2)O and D(2)O. Although no significant population of a disordered backbone state was detected at intermediate temperatures, some side chain bands not present in either the alpha-helix or beta-sheet state were observed. The observation of ROA bands in the extended amide III region assigned to beta-turns suggests that, under our experimental conditions, beta-sheet poly(L-lysine) contains up-and-down antiparallel beta-sheets based on the hairpin motif. The ROA spectrum of beta-sheet poly(L-lysine) was compared with ROA data on a number of native proteins containing different types of beta-sheet. Amide I and amide II ROA band patterns observed in beta-sheet poly(L-lysine) are different from those observed in typical beta-sheet proteins and may be characteristic of an extended flat multistranded beta-sheet, which is unlike the more irregular and twisted beta-sheet found in most proteins. However, a reduced isoform of the truncated ovine prion protein PrP(94-233) that is rich in beta-sheet shows amide I and amide II ROA bands similar to those of beta-sheet poly(L-lysine), which suggests that the C-terminal domain of the prion protein is able to support unusually flat beta-sheets. A principal component analysis (PCA) that identifies protein structural types from ROA band patterns provides a useful representation of the structural relationships among the polypeptide and protein states considered in the study.

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Section: Resultsmentioning

confidence: 98%

A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(l-lysine) to the Prion Protein

et al. 2003

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“…Crystallization of RR02rec. The purification and crystallization of this protein have been described previously (5). Briefly, RR02rec (in a solution containing 25 mM Tris-HCl and 300 mM NaCl [pH 7.5]) was concentrated to 10 mg/ml (as determined at 280 nm from the theoretical extinction coefficient 0.188) with a Centricon 10 apparatus (Millipore).…”

Section: Methodsmentioning

confidence: 99%

Crystal Structure of the Response Regulator 02 Receiver Domain, the Essential YycF Two-Component System ofStreptococcus pneumoniaein both Complexed and Native States

Bent¹,

Isaacs²,

Mitchell

et al. 2004

J Bacteriol

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“…In particular, pneumococcal RR02 being essential for viability makes it a potentially attractive target. Its biochemical characterization in vitro and structural studies may pave the way for rational drug design against this target (Bent et al, 2003(Bent et al, , 2004Clausen et al, 2003;Echenique & Trombe, 2001;Riboldi-Tunnicliffe et al, 2004;Wagner et al, 2002). However, a TCS need not be essential for viability to be a useful target.…”

Section: Pneumococcal Tcss As Antimicrobial Targetsmentioning

confidence: 99%

Role of two-component systems in the virulence of Streptococcus pneumoniae

Paterson

Blue

Mitchell

2006

Journal of Medical Microbiology

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Understanding of how the human pathogen Streptococcus pneumoniae perceives and responds to its environment in the host offers insight into the pathogenesis of disease caused by this important bacterium and the potential for improved interventions. A central role in this environmental response is played by two-component systems (TCSs), which both sense the environment and drive the cellular response. Molecular advances in the form of genome sequencing, signature-tagged mutagenesis, differential fluorescence induction and microarray analysis have yielded considerable progress in the study of these systems in S. pneumoniae. These recent advances are discussed here, focusing in particular on the role of TCSs in the virulence of S. pneumoniae.

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Cloning, overexpression, purification, crystallization and preliminary diffraction analysis of the receiver domain of MicA

Cited by 3 publications

References 5 publications

A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(l-lysine) to the Prion Protein

A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(l-lysine) to the Prion Protein

Crystal Structure of the Response Regulator 02 Receiver Domain, the Essential YycF Two-Component System ofStreptococcus pneumoniaein both Complexed and Native States

Role of two-component systems in the virulence of Streptococcus pneumoniae

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