References of "Biomolecular NMR Assignments"
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See detailBackbone and side-chain 1H, 13C, and 15N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Jean, Nicolas; Bougault, Catherine; Derouaux, Adeline ULg et al

in Biomolecular NMR Assignments (2014)

The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final biosynthetic steps ... [more ▼]

The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final biosynthetic steps of peptidoglycan synthesis from lipid II precursor and are the main targets of β-lactam antibiotics. The molecular details of peptidoglycan growth and its regulation are poorly understood. Presumably, PBPs are active in peptidoglycan synthesizing multi-enzyme complexes that are controlled from inside the cell by cytoskeletal elements. Recently, two outer-membrane lipoproteins, LpoA and LpoB, were shown to be required in Escherichia coli for the function of the main peptidoglycan synthases, PBP1A and PBP1B, by stimulating their transpeptidase activity. However, the mechanism of PBP-activation by Lpo proteins is not known, and the Lpo proteins await structural characterization at atomic resolution. Here we present the backbone and side-chain 1H, 13C, 15N NMR assignments of the N-terminal domain of LpoA from E. coli for structural and functional studies. [less ▲]

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See detailComplete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-b-lactamase and its complex with the inhibitor R-thiomandelic acid
Karsisiotis, Andreas Ioannis; Damblon, Christian ULg; Roberts, Gordon C K

in Biomolecular NMR Assignments (2014), 8

b-Lactamases inactivate b-lactam antibiotics by hydrolysis of their endocyclic b-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-b-lactamase ... [more ▼]

b-Lactamases inactivate b-lactam antibiotics by hydrolysis of their endocyclic b-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-b-lactamase enzymes are of particular concern since they are located on highly transmissible plasmids and have a broad spectrum of activity against almost all b-lactam antibiotics. We present here essentially complete ([96 %) backbone and sidechain sequence-specific NMR resonance assignments for the Bacillus cereus subclass B1 metallo-b-lactamase, BcII, and for its complex with R-thiomandelic acid, a broad spectrum inhibitor of metallo-b-lactamases. These assignments have been used as the basis for determination of the solution structures of the enzyme and its inhibitor complex and can also be used in a rapid screen for other metallo-b-lactamase inhibitors. [less ▲]

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See detail1H, 13C and 15N backbone resonance assignments for the BS3 class A beta-lactamase from Bacillus licheniformis.
Vandenameele, Julie ULg; Matagne, André ULg; Damblon, Christian ULg

in Biomolecular NMR Assignments (2010), 4(2), 195-7

Class A beta-lactamases (260-280 amino acids; M ( r ) ~ 29,000) are among the largest proteins studied in term of their folding properties. They are composed of two structural domains: an all-alpha domain ... [more ▼]

Class A beta-lactamases (260-280 amino acids; M ( r ) ~ 29,000) are among the largest proteins studied in term of their folding properties. They are composed of two structural domains: an all-alpha domain formed by five to eight helices and an alpha/beta domain consisting of a five-stranded antiparallel beta-sheet covered by three to four alpha-helices. The alpha domain (~150 residues) is made up of the central part of the polypeptide chain whereas the alpha/beta domain (111-135 residues) is constituted by the N- and C-termini of the protein. Our goal is to determine in which order the different secondary structure elements are formed during the folding of BS3. With this aim, we will use pulse-labelling hydrogen/deuterium exchange experiments, in combination with 2D-NMR measurements, to monitor the time-course of formation and stabilization of secondary structure elements. Here we report the backbone resonance assignments as the requirement for further hydrogen/deuterium exchange studies. [less ▲]

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See detailBackbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
Di Paolo, Alexandre ULg; Duval, Valerie; Matagne, André ULg et al

in Biomolecular NMR assignments (2010), 4(1), 111-4

Lysozyme from lambda bacteriophage (lambda lysozyme) is an 18 kDa globular protein displaying some of the structural features common to all lysozymes; in particular, lambda lysozyme consists of two ... [more ▼]

Lysozyme from lambda bacteriophage (lambda lysozyme) is an 18 kDa globular protein displaying some of the structural features common to all lysozymes; in particular, lambda lysozyme consists of two structural domains connected by a helix, and has its catalytic residues located at the interface between these two domains. An interesting feature of lambda lysozyme, when compared to the well-characterised hen egg-white lysozyme, is its lack of disulfide bridges; this makes lambda lysozyme an interesting system for studies of protein folding. A comparison of the folding properties of lambda lysozyme and hen lysozyme will provide important insights into the role that disulfide bonds play in the refolding pathway of the latter protein. Here we report the (1)H, (13)C and (15)N backbone resonance assignments for lambda lysozyme by heteronuclear multidimensional NMR spectroscopy. These assignments provide the starting point for detailed investigation of the refolding pathway using pulse-labelling hydrogen/deuterium exchange experiments monitored by NMR. [less ▲]

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See detail(1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein.
Vuchelen, Anneleen; O'Day, Elizabeth; De Genst, Erwin et al

in Biomolecular NMR Assignments (2009), 3(2), 231-3

Nanobodies are single chain antibodies that are uniquely produced in Camelidae, e.g. camels and llamas. They have the desirable features of small sizes (Mw < 14 kDa) and high affinities against antigens ... [more ▼]

Nanobodies are single chain antibodies that are uniquely produced in Camelidae, e.g. camels and llamas. They have the desirable features of small sizes (Mw < 14 kDa) and high affinities against antigens (Kd approximately nM), making them ideal as structural probes for biomedically relevant motifs both in vitro and in vivo. We have previously shown that nanobody binding to amyloidogenic human lysozyme variants can effectively inhibit their aggregation, the process that is at the origin of systemic amyloid disease. Here we report the NMR assignments of a new nanobody, termed NbSyn2, which recognises the C-terminus of the intrinsically disordered protein, human alpha-synuclein (aS), whose aberrant self-association is implicated in Parkinson's disease. [less ▲]

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See detail1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function.
Boudet, Julien; Chouquet, Anne; Chahboune, Aicha et al

in Biomolecular NMR assignments (2007), 1(1), 89-91

The ampG gene codes for a permease required to uptake anhydro-muropeptides into bacterial cytoplasm. Located upstream in the same operon, is another 579-base-pair-long open reading frame encoding a ... [more ▼]

The ampG gene codes for a permease required to uptake anhydro-muropeptides into bacterial cytoplasm. Located upstream in the same operon, is another 579-base-pair-long open reading frame encoding a putative lipoprotein YajG, whose nearly complete 1H,13C,15N assignments are reported here. [less ▲]

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