NMR paper Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.

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[NMR paper] Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.

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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:

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Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.

Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.

Conformation and Topology of Diacylglycerol Kinase in E.coli Membranes Revealed by Solid-state NMR Spectroscopy.

Angew Chem Int Ed Engl. 2014 Apr 2;

Authors: Chen Y, Zhang Z, Tang X, Li J, Glaubitz C, Yang J

Abstract
Solid-state NMR is a powerful tool for studying membrane proteins in a native-like lipid environment. 3D magic angle spinning (MAS) NMR was employed to characterize the structure of E.coli diacylglycerol kinase (DAGK) reconstituted into its native E.coli lipid membranes. The secondary structure and topology of DAGK revealed by solid-state NMR are different from those determined by solution-state NMR and X-ray crystallography. This study provides a good example for demonstrating the influence of membrane environments on the structure of membrane proteins.

PMID: 24700682 [PubMed - as supplied by publisher]

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