Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.

		BioNMR > Educational resources > Journal club
Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.

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

07-07-2011, 05:12 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.

Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.

Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis.

Biomol NMR Assign. 2011 Jul 6;

Authors: Veith T, Wurm JP, Duchardt-Ferner E, Weis B, Martin R, Safferthal C, Bohnsack MT, Schleiff E, Wöhnert J

Eukaryotic ribosome biogenesis requires the concerted action of ~200 auxiliary protein factors on the nascent ribosome. For many of these factors structural and functional information is still lacking. The endonuclease Nob1 has been recently identified in yeast as the enzyme responsible for the final cytoplasmatic trimming step of the pre-18S rRNA during the biogenesis of the small ribosomal subunit. Here we report the NMR resonance assignments for a Nob1 homolog from the thermophilic archeon Pyrococcus horikoshii as a prerequisite for further structural studies of this class of proteins.

PMID: 21732055 [PubMed - as supplied by publisher]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Biomol NMR Assign. 2011 Jun 7; Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...	nmrlearner	Journal club	0	06-08-2011 11:30 AM
[NMR paper] Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic t Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy. Related Articles Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy. J Biomol NMR. 2005 Apr;31(4):279-93 Authors: Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ This study reports the sequence specific chemical shifts...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c. Related Articles Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c. Protein Sci. 2003 Sep;12(9):2104-8 Authors: Liu W, Rumbley J, Englander SW, Wand AJ The mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2))...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 doma Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla. Related Articles Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla. Chembiochem. 2001 Apr 2;2(4):272-81 Authors: Pauli J, Baldus M, van Rossum B, de Groot H, Oschkinat H The backbone and side-chain 13C and 15N signals of a solid 62-residue (u-13C,15N)-labelled protein containing the alpha-spectrin SH3 domain were...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] NMR characterization of side chain flexibility and backbone structure in the type I a NMR characterization of side chain flexibility and backbone structure in the type I antifreeze protein at near freezing temperatures. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR characterization of side chain flexibility and backbone structure in the type I antifreeze protein at near freezing temperatures. Biochemistry. 1996 Dec 24;35(51):16698-704 Authors: Gronwald W, Chao H, Reddy DV, Davies PL, Sykes BD, SÃ¶nnichsen FD The flexibility of the polar side chains in the...	nmrlearner	Journal club	0	08-22-2010 02:20 PM
[NMR paper] Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Esc Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements. Related Articles Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements. Biochemistry. 1993 Jan 19;32(2):426-35 Authors: Stone MJ, Chandrasekhar K, Holmgren A, Wright PE, Dyson HJ The backbone and tryptophan side-chain dynamics of both the reduced and oxidized forms of uniformly 15N-labeled Escherichia...	nmrlearner	Journal club	0	08-21-2010 11:53 PM
[NMR paper] Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Related Articles Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Biochemistry. 1991 Sep 24;30(38):9216-28 Authors: Ikura M, Spera S, Barbato G, Kay LE, Krinks M, Bax A Heteronuclear 2D and 3D NMR experiments were carried out on recombinant Drosophila calmodulin (CaM), a protein of 148 residues and with...	nmrlearner	Journal club	0	08-21-2010 11:12 PM
[NMR paper] Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Related Articles Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Biochemistry. 1991 Sep 24;30(38):9216-28 Authors: Ikura M, Spera S, Barbato G, Kay LE, Krinks M, Bax A Heteronuclear 2D and 3D NMR experiments were carried out on recombinant Drosophila calmodulin (CaM), a protein of 148 residues and with...	nmrlearner	Journal club	0	08-21-2010 11:12 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