NMR paper Conformational changes of colicin Ia channel-forming domain upon membrane binding: a

		BioNMR > Educational resources > Journal club
[NMR paper] Conformational changes of colicin Ia channel-forming domain upon membrane binding: a

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

11-24-2010, 08:49 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,733

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

Conformational changes of colicin Ia channel-forming domain upon membrane binding: a

Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study.

Related Articles Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study.

Biochim Biophys Acta. 2002 Apr 12;1561(2):159-70

Authors: Huster D, Yao X, Jakes K, Hong M

Channel-forming colicins are bactericidal proteins that spontaneously insert into hydrophobic lipid bilayers. We have used magic-angle spinning solid-state nuclear magnetic resonance spectroscopy to examine the conformational differences between the water-soluble and the membrane-bound states of colicin Ia channel domain, and to study the effect of bound colicin on lipid bilayer structure and dynamics. We detected (13)C and (15)N isotropic chemical shift differences between the two forms of the protein, which indicate structural changes of the protein due to membrane binding. The Val C(alpha) signal, unambiguously assigned by double-quantum experiments, gave a 0.6 ppm downfield shift in the isotropic position and a 4 ppm reduction in the anisotropic chemical shift span after membrane binding. These suggest that the alpha-helices in the membrane-bound colicin adopt more ideal helical torsion angles as they spread onto the membrane. Colicin binding significantly reduced the lipid chain order, as manifested by (2)H quadrupolar couplings. These results are consistent with the model that colicin Ia channel domain forms an extended helical array at the membrane-water interface upon membrane binding.

PMID: 11997116 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli. NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli. NMR analysis reveals 17?-estradiol induced conformational change in ER? ligand binding domain expressed in E. coli. Mol Biol Rep. 2010 Dec 12; Authors: Paramanik V, Thakur MK Nuclear magnetic resonance (NMR) spectroscopy is a useful biophysical technique to study the ligand-protein interaction. In this report, we have used bacterially produced ER? and its domains for studying the functional analysis of ligand-protein interaction....	nmrlearner	Journal club	0	12-15-2010 12:03 PM
[NMR paper] Large structure rearrangement of colicin ia channel domain after membrane binding fro Large structure rearrangement of colicin ia channel domain after membrane binding from 2D 13C spin diffusion NMR. Related Articles Large structure rearrangement of colicin ia channel domain after membrane binding from 2D 13C spin diffusion NMR. J Am Chem Soc. 2005 May 4;127(17):6402-8 Authors: Luo W, Yao X, Hong M One of the main mechanisms of membrane protein folding is by spontaneous insertion into the lipid bilayer from the aqueous environment. The bacterial toxin, colicin Ia, is one such protein. To shed light on the conformational changes...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] Channel-forming membrane permeabilization by an antibacterial protein, sapecin: deter Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR. Related Articles Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR. J Biol Chem. 2004 Feb 6;279(6):4981-7 Authors: Takeuchi K, Takahashi H, Sugai M, Iwai H, Kohno T, Sekimizu K, Natori S, Shimada I The action mechanism of sapecin, an antibacterial peptide with membrane permeabilization activity, was...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9. NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9. Related Articles NMR study of Ni2+ binding to the H-N-H endonuclease domain of colicin E9. Protein Sci. 1999 Aug;8(8):1711-3 Authors: Hannan JP, Whittaker SB, Davy SL, Kühlmann UC, Pommer AJ, Hemmings AM, James R, Kleanthous C, Moore GR Ni2+ affinity columns are widely used for protein purification, but they carry the risk that Ni2+ ions may bind to the protein, either adventitiously or at a physiologically important site. Dialysis against ethylenediaminetetraacetic acid...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers. Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers. Protein Sci. 1998 Feb;7(2):342-8 Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
[NMR paper] Orientational distribution of alpha-helices in the colicin B and E1 channel domains: Orientational distribution of alpha-helices in the colicin B and E1 channel domains: a one and two dimensional 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers. Related Articles Orientational distribution of alpha-helices in the colicin B and E1 channel domains: a one and two dimensional 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers. Biochemistry. 1998 Jan 6;37(1):16-22 Authors: Lambotte S, Jasperse P, Bechinger B Thermolytic fragments of the channel-forming bacterial toxins colicin...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translo Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy. Related Articles Membrane Alignment of the Pore-Forming Component TatA(d) of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy. J Am Chem Soc. 2010 Oct 26; Authors: Walther TH, Grage SL, Roth N, Ulrich AS The twin-arginine translocase (Tat) provides protein export in bacteria and plant chloroplasts and is capable of transporting fully folded...	nmrlearner	Journal club	0	10-29-2010 07:05 PM
Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Transloca Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy Torsten H. Walther, Stephan L. Grage, Nadine Roth and Anne S. Ulrich http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja106963s/aop/images/medium/ja-2010-06963s_0001.gif Journal of the American Chemical Society DOI: 10.1021/ja106963s http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/w34WC8p2mzY	nmrlearner	Journal club	0	10-27-2010 08:51 AM

« 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