Related ArticlesSolution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.
Proteins. 2020 Sep 18;:
Authors: Fridmanis J, Otikovs M, Brangulis K, T?rs K, Jaudzems K
Abstract
Lyme disease is the most widespread vector-transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five ?-helices and an extended C-terminal loop. The fold is similar to that of Borrelia tunicate outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family. This article is protected by copyright. All rights reserved.
PMID: 32949018 [PubMed - as supplied by publisher]
A GiganticMolecular Wheel of {Gd140}:A New Member of the Molecular Wheel Family
A GiganticMolecular Wheel of {Gd140}:A New Member of the Molecular Wheel Family
Xiu-Ying Zheng, You-Hong Jiang, Gui-Lin Zhuang, Da-Peng Liu, Hong-Gang Liao, Xiang-Jian Kong, La-Sheng Long and Lan-Sun Zheng
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b11112/20171206/images/medium/ja-2017-111123_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b11112
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ue2cVW3bSqc
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[NMR paper] Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Related Articles Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A.
Biophys J. 2017 May 09;112(9):1820-1828
Authors: Kawamura T, Wakamoto T, Kitazawa S, Sakuraba S, Kameda T, Kitahara R
Abstract
Internal cavities in proteins produce conformational fluctuations and enable the binding of small ligands. Here, we report a NMR analysis of O2-binding sites by O2-induced paramagnetic...
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Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A
Analysis of O2-binding Sites in Proteins Using Gas-Pressure NMR Spectroscopy: Outer Surface Protein A
Publication date: 9 May 2017
Source:Biophysical Journal, Volume 112, Issue 9</br>
Author(s): Takahiro Kawamura, Takuro Wakamoto, Soichiro Kitazawa, Shun Sakuraba, Tomoshi Kameda, Ryo Kitahara</br>
Internal cavities in proteins produce conformational fluctuations and enable the binding of small ligands. Here, we report a NMR analysis of O2-binding sites by O2-induced paramagnetic relaxation enhancements (PREs) on amide groups of proteins in solution. Outer...
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[NMR paper] NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
Related Articles NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB.
Biochemistry. 2014 Jul 28;
Authors: Ptak CP, Hsieh CL, Lin YP, Maltsev AS, Raman R, Sharma Y, Oswald RE, Chang YF
Abstract
A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown...
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
22 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 4</br>
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Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure 15N/1H two-dimensional NMR along with high-pressure fluorescence spectroscopy. We found evidence within folded, native OspA for rapid local fluctuations of the...
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NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1137-40
Authors: Barnwal RP, Van Voorhis WC, Varani G
Abstract
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein...
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[NMR paper] NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer
NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
Related Articles NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
J Biomol NMR. 1998 May;11(4):407-14
Authors: Pham TN, Koide S
The crystal structure of outer surface protein A (OspA) from Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and it is solvent-exposed on both faces, which...
Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.
Linear Mode
