[ASAP] Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA

		BioNMR > Educational resources > Journal club
[ASAP] Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA

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

07-04-2022, 05:37 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

[ASAP] Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA

[ASAP] Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA

Denis Lacabanne, Thomas Wiegand, Margot Di Cesare, Ce?dric Orelle, Matthias Ernst, Jean-Michel Jault, Beat H. Meier, and Anja Bo?ckmann

Journal of the American Chemical Society
DOI: 10.1021/jacs.2c04287

Source: Journal of the American Chemical Society

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state ATP binding cassette (ABC) proteins are present in all phyla of life and form one of the largest protein families. The Bacillus subtilis ABC transporter BmrA is a functional homodimer that can extrude many different harmful compounds out of the cell. Each BmrA monomer is composed of a transmembrane domain (TMD) and a nucleotide binding domain (NBD). While the TMDs of ABC transporters are sequentially diverse, the highly conserved NBDs harbor...	nmrlearner	Journal club	0	01-08-2022 02:36 AM
[ASAP] Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase Jaekyun Jeon, Wai-Ming Yau, and Robert Tycko https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c11156/20201207/images/medium/ja0c11156_0007.gif Journal of the American Chemical Society DOI: 10.1021/jacs.0c11156 http://feeds.feedburner.com/~r/acs/jacsat/~4/pGPDzdJltQs	nmrlearner	Journal club	0	12-08-2020 01:36 PM
[NMR paper] Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR. Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR. J Am Chem Soc. 2013 Oct 23;135(42):15754-62 Authors: Ong YS, Lakatos A, Becker-Baldus J, Pos KM, Glaubitz C Abstract Escherichia coli EmrE, a homodimeric multidrug antiporter, has been suggested to...	nmrlearner	Journal club	0	05-29-2014 09:35 PM
Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR From The DNP-NMR Blog: Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR Ong, Y.S., et al., Detecting substrates bound to the secondary multidrug efflux pump EmrE by DNP-enhanced solid-state NMR. J Am Chem Soc, 2013. 135(42): p. 15754-62. http://www.ncbi.nlm.nih.gov/pubmed/24047229	nmrlearner	News from NMR blogs	0	01-15-2014 05:16 PM
Detecting Substrates Bound to the Secondary Multidrug Efflux Pump EmrE by DNP-Enhanced Solid-State NMR Detecting Substrates Bound to the Secondary Multidrug Efflux Pump EmrE by DNP-Enhanced Solid-State NMR Yean Sin Ong, Andrea Lakatos, Johanna Becker-Baldus, Klaas M. Pos and Clemens Glaubitz http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja402605s/aop/images/medium/ja-2013-02605s_0006.gif Journal of the American Chemical Society DOI: 10.1021/ja402605s http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/AjOxCwRFsQs	nmrlearner	Journal club	0	10-12-2013 12:59 AM
[NMR paper] Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy. Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy. Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy. Angew Chem Int Ed Engl. 2013 Aug 12; Authors: Gayen A, Banigan JR, Traaseth NJ Abstract An EmrE-ging market: Oriented solid-state NMR spectroscopy and biochemical cross-linking experiments were used to show that the ligand-free membrane protein transporter EmrE forms...	nmrlearner	Journal club	0	08-14-2013 05:24 PM
[NMR paper] Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies. Related Articles Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies. FEBS Lett. 2004 Jun 18;568(1-3):117-21 Authors: Mason AJ, Siarheyeva A, Haase W, Lorch M, van Veen H, Glaubitz C The ABC transporter LmrA in Lactococcus lactis confers resistance to a wide range of antibiotics and cytotoxic drugs and is a functional homologue of P-glycoprotein. Recently, solid-state NMR...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] NMR investigation of the multidrug transporter EmrE, an integral membrane protein. NMR investigation of the multidrug transporter EmrE, an integral membrane protein. Related Articles NMR investigation of the multidrug transporter EmrE, an integral membrane protein. Eur J Biochem. 1998 Jun 15;254(3):610-9 Authors: Schwaiger M, Lebendiker M, Yerushalmi H, Coles M, Gröger A, Schwarz C, Schuldiner S, Kessler H EmrE is an Escherichia coli multidrug transport protein that confers resistance to a wide range of toxicants by active transport across the bacterial cell membrane. The highly hydrophobic polytopic integral membrane...	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