NMR paper Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

		BioNMR > Educational resources > Journal club
[NMR paper] Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

09-21-2020, 05:44 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,776

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.

Related Articles Solution 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]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
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	nmrlearner	Journal club	0	12-07-2017 11:34 AM
[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...	nmrlearner	Journal club	0	05-13-2017 02:08 PM
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...	nmrlearner	Journal club	0	05-10-2017 06:52 AM
[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...	nmrlearner	Journal club	0	07-30-2014 10:22 AM
[NMR paper] Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct ?-helical architecture and provides first structural representative of protein domain family PF14203. Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct ?-helical architecture and provides first structural representative of protein domain family PF14203. Related Articles Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct ?-helical architecture and provides first structural representative of protein domain family PF14203. J Struct Funct Genomics. 2013 Sep 19; Authors: Pulavarti SV, Eletsky A, Lee HW, Acton TB, Xiao R, Everett JK, Prestegard JH, Montelione GT, Szyperski T ...	nmrlearner	Journal club	0	09-21-2013 06:50 PM
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> </br> 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...	nmrlearner	Journal club	0	02-03-2013 10:13 AM
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...	nmrlearner	Journal club	0	09-10-2011 06:51 PM
[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...	nmrlearner	Journal club	0	11-17-2010 11:06 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off