NMR paper Channel-forming membrane permeabilization by an antibacterial protein, sapecin: deter

		BioNMR > Educational resources > Journal club
[NMR paper] Channel-forming membrane permeabilization by an antibacterial protein, sapecin: deter

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, 09:16 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,734

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

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 investigated. The dose dependence of the membrane permeabilization caused by sapecin was sigmoidal, suggesting that sapecin oligomerization leads to the membrane permeabilization. Solution nuclear magnetic resonance analysis of the sapecin-phospholipid vesicle complex revealed the surface buried in the membrane and oligomerization surface on the sapecin molecule. The membrane-buried surface of sapecin was determined by observing the transferred cross-saturation phenomena from the alkyl chains of the phospholipid vesicle to the amide protons of sapecin. The membrane-buried surface contains basic and highly exposed hydrophobic residues, which are suitable for interacting with the acidic bacterial membrane. The oligomerization surface was also identified by comparisons between the results from hydrogen-deuterium exchange experiments and transferred cross-saturation experiments. On the basis of the results from the NMR experiments we built a putative model of sapecin oligomers, which provides insights into the membrane permeabilization caused by insect defensins.

PMID: 14630928 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. J Biol Chem. 2011 Jul 8;286(27):24394-406 Authors: Bhunia A, Saravanan R, Mohanram H, Mangoni ML, Bhattacharjya S Abstract Temporins are a group of closely related short...	nmrlearner	Journal club	0	09-09-2011 06:42 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] NMR evidence for independent domain structures in zoocin A, an antibacterial exoenzym NMR evidence for independent domain structures in zoocin A, an antibacterial exoenzyme. Related Articles NMR evidence for independent domain structures in zoocin A, an antibacterial exoenzyme. Biochem Biophys Res Commun. 2004 Apr 30;317(2):527-30 Authors: Liang Q, Simmonds RS, Timkovich R NMR was used to obtain spectroscopic evidence supporting a two domain model for zoocin A in which an N-terminal catalytic domain is linked by a threonine-proline rich linker to a target recognition domain responsible for recognizing the cell wall of bacteria...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] 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...	nmrlearner	Journal club	0	11-24-2010 08:49 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
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
NMR structure and ion channel activity of the p7 protein from hepatitis C virus. NMR structure and ion channel activity of the p7 protein from hepatitis C virus. Related Articles NMR structure and ion channel activity of the p7 protein from hepatitis C virus. J Biol Chem. 2010 Jul 28; Authors: Montserret R, Saint N, Vanbelle C, Salvay AG, Simorre JP, Ebel C, Sapay N, Renisio JG, Bockmann A, Steinmann E, Pietschmann T, Dubuisson J, Chipot C, Penin F The small membrane protein p7 of hepatitis C virus forms oligomers and exhibits ion channel activity essential for virus infectivity. These viroporin features render p7 an...	nmrlearner	Journal club	0	08-17-2010 03:36 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