NMR paper Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel

		BioNMR > Educational resources > Journal club
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel

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

11-17-2010, 11:06 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

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 residue C-terminal colicin E1 channel domain is the largest polypeptide to have been characterized by 15N solid-state NMR spectroscopy in oriented membrane bilayers. The 15N-NMR spectra of the colicin E1 show that: (1) the structure and dynamics are independent of anionic lipid content in both oriented and unoriented samples; (2) assuming the secondary structure of the polypeptide is helical, there are both trans-membrane and in-plane helical segments; (3) trans-membrane helices account for approximately 20-25% of the channel polypeptide, which is equivalent to 38-48 residues of the 190-residue polypeptide. The results of the two-dimensional PISEMA spectrum are interpreted in terms of a single trans-membrane helical hairpin inserted into the bilayer from each channel molecule. These data are also consistent with this helical hairpin being derived from the 38-residue hydrophobic segment near the C-terminus of the colicin E1 channel polypeptide.

PMID: 9521110 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Combined Use of Replica-Exchange Molecular Dynamics and Magic-Angle-Spinning Solid-State NMR Spectral Simulations for Determining the Structure and Orientation of Membrane-Bound Peptide. Combined Use of Replica-Exchange Molecular Dynamics and Magic-Angle-Spinning Solid-State NMR Spectral Simulations for Determining the Structure and Orientation of Membrane-Bound Peptide. Combined Use of Replica-Exchange Molecular Dynamics and Magic-Angle-Spinning Solid-State NMR Spectral Simulations for Determining the Structure and Orientation of Membrane-Bound Peptide. J Phys Chem B. 2011 Jun 13; Authors: Ikeda K, Kameda T, Harada E, Akutsu H, Fujiwara T We report an approach to determining membrane-peptides and -protein complex structures by...	nmrlearner	Journal club	0	06-15-2011 01:15 PM
NMR structure of CaBP1 in a Ca(2+) -bound closed state: Implications for target recognition. NMR structure of CaBP1 in a Ca(2+) -bound closed state: Implications for target recognition. NMR structure of CaBP1 in a Ca(2+) -bound closed state: Implications for target recognition. Protein Sci. 2011 May 23; Authors: Park S, Li C, Ames JB Calcium binding protein 1 (CaBP1), a neuron-specific member of the calmodulin (CaM) superfamily, regulates the Ca(2+) dependent activity of inositol 1,4,5-triphosphate receptors (InsP3Rs) and various voltage-gated Ca(2+) channels. Here we present the NMR structure of full-length CaBP1 with Ca(2+) bound at the...	nmrlearner	Journal club	0	05-25-2011 07:01 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] Solid-state NMR spectroscopic studies of an integral membrane protein inserted into a Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays. Related Articles Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays. J Am Chem Soc. 2004 Aug 11;126(31):9504-5 Authors: Lorigan GA, Dave PC, Tiburu EK, Damodaran K, Abu-Baker S, Karp ES, Gibbons WJ, Minto RE This communication demonstrates for the first time that solid-state NMR spectroscopic studies can be used to investigate aligned...	nmrlearner	Journal club	0	11-24-2010 10:01 PM
[NMR paper] Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals to Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with amino acid residues. Related Articles Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with amino acid residues. Magn Reson Chem. 2004 Feb;42(2):218-30 Authors: Saitô H, Mikami J, Yamaguchi S, Tanio M, Kira A, Arakawa T, Yamamoto K, Tuzi S We have so...	nmrlearner	Journal club	0	11-24-2010 09:25 PM
[NMR paper] The closed state of a H+ channel helical bundle combining precise orientational and d The closed state of a H+ channel helical bundle combining precise orientational and distance restraints from solid state NMR. Related Articles The closed state of a H+ channel helical bundle combining precise orientational and distance restraints from solid state NMR. Biochemistry. 2002 Nov 5;41(44):13170-7 Authors: Nishimura K, Kim S, Zhang L, Cross TA An interhelical distance has been precisely measured by REDOR solid-state NMR spectroscopy in the transmembrane tetrameric bundle of M2-TMP, from the M2 proton channel of the influenza A viral...	nmrlearner	Journal club	0	11-24-2010 08:58 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 investigation of the dynamics of the soluble and membrane-bound colic Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain. Related Articles Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain. Biochemistry. 2001 Jun 26;40(25):7662-74 Authors: Huster D, Xiao L, Hong M Solid-state NMR spectroscopy was employed to study the molecular dynamics of the colicin Ia channel domain in the soluble and membrane-bound states. In the soluble state, the protein executes small-amplitude librations (with...	nmrlearner	Journal club	0	11-19-2010 08:32 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