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Ribosome PDB id
1r73
Jmol
Contents
Protein chain
66 a.a. *
* Residue conservation analysis
PDB id:
1r73
Name: Ribosome
Title: Solution structure of tm1492, the l29 ribosomal protein from thermotoga maritima
Structure: 50s ribosomal protein l29. Chain: a. Synonym: tm1492
Source: Thermotoga maritima. Organism_taxid: 2336
NMR struc: 20 models
Authors: W.Peti,T.Etezady-Esfarjani,T.Herrmann,H.E.Klock,S.A.Lesley, K.Wuethrich,Joint Center For Structural Genomics (Jcsg)
Key ref: W.Peti et al. (2004). NMR for structural proteomics of Thermotoga maritima: screening and structure determination. J Struct Funct Genomics, 5, 205-215. PubMed id: 15263836 DOI: 10.1023/B:JSFG.0000029055.84242.9f
Date:
17-Oct-03     Release date:   10-Aug-04    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P38514  (RL29_THEMA) -  50S ribosomal protein L29
Seq:
Struc: 		66 a.a.
66 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   3 terms 
  Biological process     translation   1 term 
  Biochemical function     structural constituent of ribosome     1 term  

 

 
DOI no: 10.1023/B:JSFG.0000029055.84242.9f J Struct Funct Genomics 5:205-215 (2004)
PubMed id: 15263836  
 
 
NMR for structural proteomics of Thermotoga maritima: screening and structure determination.
W.Peti, T.Etezady-Esfarjani, T.Herrmann, H.E.Klock, S.A.Lesley, K.Wüthrich.
 
  ABSTRACT  
 
This paper describes the NMR screening of 141 small (<15 kDa) recombinant Thermotoga maritima proteins for globular folding. The experimental data shows that approximately 25% of the screened proteins are folded under our screening conditions, which makes this procedure an important step for selecting those proteins that are suitable for structure determination. A comparison of screening based either on 1D 1H NMR with unlabeled proteins or on 2D [1H,15N]-COSY with uniformly 15N-labeled proteins is presented, and a comprehensive analysis of the 1D 1H NMR screening data is described. As an illustration of the utility of these methods to structural proteomics, the NMR structure determination of TM1492 (ribosomal protein L29) is presented. This 66-residue protein consists of a N-terminal 3(10)-helix and two long alpha-helices connected by a tight turn centered about glycine 35, where conserved leucine and isoleucine residues in the two alpha-helices form a small hydrophobic core.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20073081 D.R.Jensen, C.Woytovich, M.Li, P.Duvnjak, M.S.Cassidy, R.O.Frederick, L.F.Bergeman, F.C.Peterson, and B.F.Volkman (2010).
Rapid, robotic, small-scale protein production for NMR screening and structure determination.
  Protein Sci, 19, 570-578.
PDB code: 2kom
17563834 F.E.Jenney, and M.W.Adams (2008).
The impact of extremophiles on structural genomics (and vice versa).
  Extremophiles, 12, 39-50.  
17165694 K.G.Valentine, M.S.Pometun, J.M.Kielec, R.E.Baigelman, J.K.Staub, K.L.Owens, and A.J.Wand (2006).
Magnetic susceptibility-induced alignment of proteins in reverse micelles.
  J Am Chem Soc, 128, 15930-15931.  
16618368 K.Peng, P.Radivojac, S.Vucetic, A.K.Dunker, and Z.Obradovic (2006).
Length-dependent prediction of protein intrinsic disorder.
  BMC Bioinformatics, 7, 208.  
16597824 L.Columbus, J.Lipfert, H.Klock, I.Millett, S.Doniach, and S.A.Lesley (2006).
Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination.
  Protein Sci, 15, 961-975.  
16505959 T.Etezady-Esfarjani, T.Herrmann, R.Horst, and K.Wüthrich (2006).
Automated protein NMR structure determination in crude cell-extract.
  J Biomol NMR, 34, 3.  
16271892 F.Schlünzen, D.N.Wilson, P.Tian, J.M.Harms, S.J.McInnes, H.A.Hansen, R.Albrecht, J.Buerger, S.M.Wilbanks, and P.Fucini (2005).
The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction.
  Structure, 13, 1685-1694.
PDB code: 2d3o
15937903 L.Columbus, W.Peti, T.Etezady-Esfarjani, T.Herrmann, and K.Wüthrich (2005).
NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.
  Proteins, 60, 552-557.
PDB code: 1t3v
16199668 M.S.Almeida, T.Herrmann, W.Peti, I.A.Wilson, and K.Wüthrich (2005).
NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins.
  Protein Sci, 14, 2880-2886.
PDB codes: 1uwd 1wcj
16211521 R.Page, A.M.Deacon, S.A.Lesley, and R.C.Stevens (2005).
Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins.
  J Struct Funct Genomics, 6, 209-217.  
15677718 R.Page, W.Peti, I.A.Wilson, R.C.Stevens, and K.Wüthrich (2005).
NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.
  Proc Natl Acad Sci U S A, 102, 1901-1905.  
16222553 T.Luan, V.Jaravine, A.Yee, C.H.Arrowsmith, and V.Y.Orekhov (2005).
Optimization of resolution and sensitivity of 4D NOESY using multi-dimensional decomposition.
  J Biomol NMR, 33, 1.  
16188992 W.Peti, M.A.Johnson, T.Herrmann, B.W.Neuman, M.J.Buchmeier, M.Nelson, J.Joseph, R.Page, R.C.Stevens, P.Kuhn, and K.Wüthrich (2005).
Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.
  J Virol, 79, 12905-12913.
PDB code: 1ysy
16283429 W.Peti, R.Page, K.Moy, M.O'Neil-Johnson, I.A.Wilson, R.C.Stevens, and K.Wüthrich (2005).
Towards miniaturization of a structural genomics pipeline using micro-expression and microcoil NMR.
  J Struct Funct Genomics, 6, 259-267.  
15723348 W.Peti, T.Herrmann, O.Zagnitko, S.K.Grzechnik, and K.Wüthrich (2005).
NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.
  Proteins, 59, 387-390.
PDB code: 1rhx
16187360 Z.Obradovic, K.Peng, S.Vucetic, P.Radivojac, and A.K.Dunker (2005).
Exploiting heterogeneous sequence properties improves prediction of protein disorder.
  Proteins, 61, 176-182.  
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.