Author response for "Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family"

2020 ◽  
Author(s):  
Jēkabs Fridmanis ◽  
Mārtiņš Otikovs ◽  
Kalvis Brangulis ◽  
Kaspars Tārs ◽  
Kristaps Jaudzems
Keyword(s):  
Borrelia Burgdorferi ◽  
Outer Surface ◽  
Protein Family ◽  
Nmr Structure ◽  
Solution Nmr ◽  
Author Response

scholarly journals Structural and Functional Analysis of BBA03, Borrelia burgdorferi Competitive Advantage Promoting Outer Surface Lipoprotein

Pathogens ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 826
Author(s):  
Jēkabs Fridmanis ◽  
Raitis Bobrovs ◽  
Kalvis Brangulis ◽  
Kaspars Tārs ◽  
Kristaps Jaudzems
Keyword(s):  
Borrelia Burgdorferi ◽  
Competitive Advantage ◽  
Outer Surface ◽  
Solution Nmr ◽  
Mammalian Host ◽  
Tick Vector ◽  
Evolutionary Relatedness ◽  
Relatedness Analysis ◽  
Linear Plasmid 54

BBA03 is a Borrelia burgdorferi outer surface lipoprotein encoded on one of the most conserved plasmids in Borrelia genome, linear plasmid 54 (lp54). Although many of its genes have been identified as contributing or essential for spirochete fitness in vivo, the majority of the proteins encoded on this plasmid have no known function and lack homologs in other organisms. In this paper, we report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBA03, which is known to provide a competitive advantage to the bacteria during the transmission from tick vector to mammalian host. BBA03 shows structural homology to other outer surface lipoproteins reflecting their genetic and evolutionary relatedness. Analysis of the structure reveals a pore in BBA03, which could potentially bind lipids.

Solution NMR structure of titin N2A region Ig domain I83 and its interaction with metal ions

2021 ◽  
pp. 166977
Author(s):  
Colleen Kelly ◽  
Nicola Pace ◽  
Matthew Gage ◽  
Mark Pfuhl
Keyword(s):  
Metal Ions ◽  
Nmr Structure ◽  
Solution Nmr ◽  
Ig Domain

scholarly journals Solution NMR Structure of the Ca2+-bound N-terminal Domain of CaBP7

2012 ◽  
Vol 287 (45) ◽  
pp. 38231-38243 ◽  
Author(s):  
Hannah V. McCue ◽  
Pryank Patel ◽  
Andrew P. Herbert ◽  
Lu-Yun Lian ◽  
Robert D. Burgoyne ◽  
...  
Keyword(s):  
Nmr Structure ◽  
Solution Nmr ◽  
Terminal Domain

scholarly journals NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e5412 ◽  
Author(s):  
Jesper S. Oeemig ◽  
O.H. Samuli Ollila ◽  
Hideo Iwaï
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Structural Changes ◽  
Nmr Structure ◽  
Dynamics Simulation ◽  
Solution Nmr ◽  
Gram Negative Bacteria ◽  
E Coli ◽  
Terminal Domain ◽  
Tonb Protein ◽  
Monomeric Structure

The TonB protein plays an essential role in the energy transduction system to drive active transport across the outer membrane (OM) using the proton-motive force of the cytoplasmic membrane of Gram-negative bacteria. The C-terminal domain (CTD) of TonB protein is known to interact with the conserved TonB box motif of TonB-dependent OM transporters, which likely induces structural changes in the OM transporters. Several distinct conformations of differently dissected CTDs of Escherichia coli TonB have been previously reported. Here we determined the solution NMR structure of a 96-residue fragment of Pseudomonas aeruginosa TonB (PaTonB-96). The structure shows a monomeric structure with the flexible C-terminal region (residues 338–342), different from the NMR structure of E. coli TonB (EcTonB-137). The extended and flexible C-terminal residues are confirmed by 15N relaxation analysis and molecular dynamics simulation. We created models for the PaTonB-96/TonB box interaction and propose that the internal fluctuations of PaTonB-96 makes it more accessible for the interactions with the TonB box and possibly plays a role in disrupting the plug domain of the TonB-dependent OM transporters.

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