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PDBsum entry 2eya

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protein links
Plant protein PDB id
2eya
Jmol
Contents
Protein chain
46 a.a. *
* Residue conservation analysis
PDB id:
2eya
Name: Plant protein
Title: Dmso refined solution structure of crambin in acetone/water
Structure: Crambin. Chain: a. Engineered: yes
Source: Crambe hispanica subsp. Abyssinica. Organism_taxid: 3721. Strain: subsp. Abyssinica. Gene: thi2. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: H.C.Ahn,J.L.Markley
Key ref: H.C.Ahn et al. (2006). Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface. J Am Chem Soc, 128, 4398-4404. PubMed id: 16569017 DOI: 10.1021/ja057773d
Date:
09-Nov-05     Release date:   23-May-06    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01542  (CRAM_CRAAB) -  Crambin
Seq:
Struc:
46 a.a.
46 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     defense response   1 term 

 

 
DOI no: 10.1021/ja057773d J Am Chem Soc 128:4398-4404 (2006)
PubMed id: 16569017  
 
 
Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface.
H.C.Ahn, N.Juranić, S.Macura, J.L.Markley.
 
  ABSTRACT  
 
We chose crambin, a hydrophobic and water-insoluble protein originally isolated from the seeds of the plant Crambe abyssinica, as a model for NMR investigations of membrane-associated proteins. We produced isotopically labeled crambin(P22,L25) (variant of crambin containing Pro22 and Leu25) as a cleavable fusion with staphylococcal nuclease and refolded the protein by an approach that has proved successful for the production of proteins with multiple disulfide bonds. We used NMR spectroscopy to determine the three-dimensional structure of the protein in two membrane-mimetic environments: in a mixed aqueous-organic solvent (75%/25%, acetone/water) and in DPC micelles. With the sample in the mixed solvent, it was possible to determine (>NH...OC<) hydrogen bonds directly by the detection of (h3)J(NC)' couplings. H-bonds determined in this manner were utilized in the refinement of the NMR-derived protein structures. With the protein in DPC (dodecylphosphocholine) micelles, we used manganous ion as an aqueous paramagnetic probe to determine the surface of crambin that is shielded by the detergent. With the exception of the aqueous solvent exposed loop containing residues 20 and 21, the protein surface was protected by DPC. This suggests that the protein may be similarly embedded in physiological membranes. The strategy described here for the expression and structure determination of crambin should be applicable to structural and functional studies of membrane active toxins and small membrane proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20042596 S.A.Dames (2010).
Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles.
  J Biol Chem, 285, 7766-7775.
PDB codes: 2kio 2kit
18618697 A.Bhunia, P.N.Domadia, H.Mohanram, and S.Bhattacharjya (2009).
NMR structural studies of the Ste11 SAM domain in the dodecyl phosphocholine micelle.
  Proteins, 74, 328-343.  
19562114 D.Bang, V.Tereshko, A.A.Kossiakoff, and S.B.Kent (2009).
Role of a salt bridge in the model protein crambin explored by chemical protein synthesis: X-ray structure of a unique protein analogue, [V15A]crambin-alpha-carboxamide.
  Mol Biosyst, 5, 750-756.
PDB codes: 2fd7 2fd9
19034675 R.Schmucki, S.Yokoyama, and P.Güntert (2009).
Automated assignment of NMR chemical shifts using peak-particle dynamics simulation with the DYNASSIGN algorithm.
  J Biomol NMR, 43, 97.  
18305196 N.Juranić, J.J.Dannenberg, G.Cornilescu, P.Salvador, E.Atanasova, H.C.Ahn, S.Macura, J.L.Markley, and F.G.Prendergast (2008).
Structural dependencies of protein backbone 2JNC' couplings.
  Protein Sci, 17, 768-776.  
17584791 K.G.Tina, R.Bhadra, and N.Srinivasan (2007).
PIC: Protein Interactions Calculator.
  Nucleic Acids Res, 35, W473-W476.  
17567747 N.Juranić, E.Atanasova, J.H.Streiff, S.Macura, and F.G.Prendergast (2007).
Solvent-induced differentiation of protein backbone hydrogen bonds in calmodulin.
  Protein Sci, 16, 1329-1337.  
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 codes are shown on the right.