PDBsum entry 1c0c

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protein ligands links
Hydrolase PDB id
Protein chain
124 a.a. *
SO4 ×3
Waters ×2
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Bovine pancreatic ribonuclease a desiccated for 4.0 days
Structure: Ribonuclease a. Chain: a. Ec:
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: pancreas
2.00Å     R-factor:   0.190     R-free:   0.268
Authors: J.A.Bell
Key ref: J.A.Bell (1999). X-ray crystal structures of a severely desiccated protein. Protein Sci, 8, 2033-2040. PubMed id: 10548049 DOI: 10.1110/ps.8.10.2033
15-Jul-99     Release date:   14-Oct-99    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P61823  (RNAS1_BOVIN) -  Ribonuclease pancreatic
150 a.a.
124 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Pancreatic ribonuclease.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     nucleic acid binding     1 term  


DOI no: 10.1110/ps.8.10.2033 Protein Sci 8:2033-2040 (1999)
PubMed id: 10548049  
X-ray crystal structures of a severely desiccated protein.
Unlike most protein crystals, form IX of bovine pancreatic ribonuclease A diffracts well when severely dehydrated. Crystal structures have been solved after 2.5 and 4 days of desiccation with CaSO4, at 1.9 and 2.0 A resolution, respectively. The two desiccated structures are very similar. An RMS displacement of 1.6 A is observed for main-chain atoms in each structure when compared to the hydrated crystal structure with some large rearrangements observed in loop regions. The structural changes are the result of intermolecular contacts formed by strong electrostatic interactions in the absence of a high dielectric medium. The electron density is very diffuse for some surface loops, consistent with a very disordered structure. This disorder is related to the conformational changes. These results help explain conformational changes during the lyophilization of protein and the associated phenomena of denaturation and molecular memory.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20798314 J.Rabone, Y.F.Yue, S.Y.Chong, K.C.Stylianou, J.Bacsa, D.Bradshaw, G.R.Darling, N.G.Berry, Y.Z.Khimyak, A.Y.Ganin, P.Wiper, J.B.Claridge, and M.J.Rosseinsky (2010).
An adaptable peptide-based porous material.
  Science, 329, 1053-1057.  
20169168 V.Gupta, R.K.Gupta, G.Khare, D.M.Salunke, A.Surolia, and A.K.Tyagi (2010).
Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration.
  PLoS One, 5, e9222.
PDB codes: 3l1a 3l2z
17044066 B.L.Simons, H.Kaplan, S.M.Fournier, T.Cyr, and M.A.Hefford (2007).
A novel cross-linked RNase A dimer with enhanced enzymatic properties.
  Proteins, 66, 183-195.  
16552138 K.Harata, and T.Akiba (2006).
Structural phase transition of monoclinic crystals of hen egg-white lysozyme.
  Acta Crystallogr D Biol Crystallogr, 62, 375-382.
PDB codes: 2d4i 2d4j 2d4k
15965985 J.J.Hill, E.Y.Shalaev, and G.Zografi (2005).
Thermodynamic and dynamic factors involved in the stability of native protein structure in amorphous solids in relation to levels of hydration.
  J Pharm Sci, 94, 1636-1667.  
15039550 K.Harata, and T.Akiba (2004).
Phase transition of triclinic hen egg-white lysozyme crystal associated with sodium binding.
  Acta Crystallogr D Biol Crystallogr, 60, 630-637.
PDB codes: 1v7s 1v7t
12876340 G.D.Smith, and R.H.Blessing (2003).
Lessons from an aged, dried crystal of T(6) human insulin.
  Acta Crystallogr D Biol Crystallogr, 59, 1384-1394.
PDB codes: 1os3 1os4
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