NMR paper NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.

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[NMR paper] NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.

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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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05-20-2014, 11:10 PM

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NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.

NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.

Related Articles NMR structures of ?-proteobacterial ATPase-regulating ?-subunits.

J Mol Biol. 2014 May 13;

Authors: Serrano P, Geralt M, Mohanty B, Wüthrich K

Abstract
NMR structures of ?-subunits, which are recently discovered ?-proteobacterial F1F0-ATPase regulatory proteins representing a Pfam protein family of 246 sequences from 219 species (PF07345), exhibit a four-helix bundle, which is different from all other known F1F0-ATPase inhibitors. Chemical shift mapping reveals a conserved ADP/ATP-binding site in ?-subunit, which mediates long-range conformational changes related to function, as revealed by the structure of the Paracoccus denitrificans ?-subunit in complex with ADP. These structural data suggest a new mechanism of F1F0-ATPase regulation in ?-proteobacteria.

PMID: 24838125 [PubMed - as supplied by publisher]

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