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PDBsum entry 2jzz
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Signaling protein PDB id
2jzz

 

 

 

 

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Contents
Protein chain
76 a.a. *
* Residue conservation analysis
PDB id:
2jzz
Name: Signaling protein
Title: Solid-state nmr structure of microcrystalline ubiquitin
Structure: Ubiquitin. Chain: a
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 20 models
Authors: T.Manolikas,T.Herrmann,B.H.Meier
Key ref: T.Manolikas et al. (2008). Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy. J Am Chem Soc, 130, 3959-3966. PubMed id: 18321098
Date:
22-Jan-08     Release date:   25-Mar-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		685 a.a.
76 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Am Chem Soc 130:3959-3966 (2008)
PubMed id: 18321098  
 
 
Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy.
T.Manolikas, T.Herrmann, B.H.Meier.
 
  ABSTRACT  
 
Proton-driven 13C spin diffusion (PDSD) is a simple and robust two-dimensional NMR experiment. It leads to spectra with a high signal-to-noise ratio in which cross-peaks contain information about internuclear distances. We show that the total information content is sufficient to determine the atomic-resolution structure of a small protein from a single, uniformly 13C-, 15N-labeled microcrystalline sample. For the example of ubiquitin, the structure was determined by a manual procedure followed by an automatic optimization of the manual structure as well as by a fully automated structure determination approach. The relationship between internuclear distances and cross-peak intensities in the spectra is investigated.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20609396 C.Noirot, B.Habenstein, L.Bousset, R.Melki, B.H.Meier, Y.Endo, F.Penin, and A.Böckmann (2011).
Wheat-germ cell-free production of prion proteins for solid-state NMR structural studies.
  N Biotechnol, 28, 232-238.  
21384999 G.D.Paëpe, J.R.Lewandowski, A.Loquet, M.Eddy, S.Megy, A.Böckmann, and R.G.Griffin (2011).
Heteronuclear proton assisted recoupling.
  J Chem Phys, 134, 095101.  
21431110 J.N.Dumez, and L.Emsley (2011).
A master-equation approach to the description of proton-driven spin diffusion from crystal geometry using simulated zero-quantum lineshapes.
  Phys Chem Chem Phys, 13, 7363-7370.  
21432937 K.Y.Huang, G.A.Amodeo, L.Tong, and A.McDermott (2011).
The structure of human ubiquitin in 2-methyl-2,4-pentanediol: a new conformational switch.
  Protein Sci, 20, 630-639.
PDB code: 3ons
21214861 M.Bieri, A.H.Kwan, M.Mobli, G.F.King, J.P.Mackay, and P.R.Gooley (2011).
Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination.
  FEBS J, 278, 704-715.  
21442705 M.Huber, S.Hiller, P.Schanda, M.Ernst, A.Böckmann, R.Verel, and B.H.Meier (2011).
A proton-detected 4D solid-state NMR experiment for protein structure determination.
  Chemphyschem, 12, 915-918.
PDB code: 2l3z
21034466 A.F.Angyán, B.Szappanos, A.Perczel, and Z.Gáspári (2010).
CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.
  BMC Struct Biol, 10, 39.  
20572250 A.Schuetz, C.Wasmer, B.Habenstein, R.Verel, J.Greenwald, R.Riek, A.Böckmann, and B.H.Meier (2010).
Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).
  Chembiochem, 11, 1543-1551.  
20633348 S.Cavadini (2010).
Indirect detection of nitrogen-14 in solid-state NMR spectroscopy.
  Prog Nucl Magn Reson Spectrosc, 56, 46-77.  
20711561 S.Paasch, and E.Brunner (2010).
Trends in solid-state NMR spectroscopy and their relevance for bioanalytics.
  Anal Bioanal Chem, 398, 2351-2362.  
19779834 A.Böckmann, C.Gardiennet, R.Verel, A.Hunkeler, A.Loquet, G.Pintacuda, L.Emsley, B.H.Meier, and A.Lesage (2009).
Characterization of different water pools in solid-state NMR protein samples.
  J Biomol NMR, 45, 319-327.  
19652822 A.Lesage (2009).
Recent advances in solid-state NMR spectroscopy of spin I = 1/2 nuclei.
  Phys Chem Chem Phys, 11, 6876-6891.  
19245337 A.McDermott (2009).
Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR.
  Annu Rev Biophys, 38, 385-403.  
19334788 J.R.Lewandowski, G.De Paëpe, M.T.Eddy, and R.G.Griffin (2009).
(15)N-(15)N proton assisted recoupling in magic angle spinning NMR.
  J Am Chem Soc, 131, 5769-5776.  
19530792 L.A.Straasø, M.Bjerring, N.Khaneja, and N.C.Nielsen (2009).
Multiple-oscillating-field techniques for accurate distance measurements by solid-state NMR.
  J Chem Phys, 130, 225103.  
  19562810 M.J.Bayro, T.Maly, N.R.Birkett, C.M.Dobson, and R.G.Griffin (2009).
Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy.
  Angew Chem Int Ed Engl, 48, 5708-5710.  
19419167 S.Sharif, M.Singh, S.J.Kim, and J.Schaefer (2009).
Staphylococcus aureus peptidoglycan tertiary structure from carbon-13 spin diffusion.
  J Am Chem Soc, 131, 7023-7030.  
19034676 Y.Shen, R.Vernon, D.Baker, and A.Bax (2009).
De novo protein structure generation from incomplete chemical shift assignments.
  J Biomol NMR, 43, 63-78.  
19123534 G.De Paëpe, J.R.Lewandowski, A.Loquet, A.Böckmann, and R.G.Griffin (2008).
Proton assisted recoupling and protein structure determination.
  J Chem Phys, 129, 245101.  
18988744 S.Balayssac, I.Bertini, A.Bhaumik, M.Lelli, and C.Luchinat (2008).
Paramagnetic shifts in solid-state NMR of proteins to elicit structural information.
  Proc Natl Acad Sci U S A, 105, 17284-17289.
PDB code: 2k9c
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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