NMR paper Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.

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[NMR paper] Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.

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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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12-25-2013, 03:39 PM

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Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.

Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.

Related Articles Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.

Biomol NMR Assign. 2013 Dec 24;

Authors: Castellen P, Sforça ML, Gueiros-Filho FJ, de Mattos Zeri AC

Abstract
Bacterial cell division proteins must assemble at the middle of the cell to ensure the viability of both daughter cells. The first step in the assembly of the cell division apparatus is the polymerization of the tubulin-like protein FtsZ into a ring-shaped scaffold, the Z-ring. The Min system contributes to the spatial precision of division by inhibiting FtsZ polymerization at the cell poles. The component of this system that interacts with FtsZ is MinC, a 25*kDa protein that has two domains. The N-terminal domain of MinC is the main responsible for FtsZ inhibition, being sufficient to block Z-ring assembly when overexpressed in vivo, and to inhibit FtsZ polymerization in vitro. Despite intensive studies, little is known about the MinC binding site for FtsZ. We have assigned the backbone and side chain resonances of the MinC N-terminal domain of Bacillus subtilis through NMR spectroscopy. These assignments provide the basis to characterize the interaction between the N-terminal domain of MinC and FtsZ by NMR methods.

PMID: 24366721 [PubMed - as supplied by publisher]

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