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PDBsum entry 1rsm

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Hydrolase (nucleic acid,RNA) PDB id
1rsm
Jmol
Contents
Protein chain
124 a.a. *
Ligands
NIN
Waters ×75
* Residue conservation analysis
PDB id:
1rsm
Name: Hydrolase (nucleic acid,RNA)
Title: The 2-angstroms resolution structure of a thermostable ribonuclease a chemically cross-linked between lysine residues 7 and 41
Structure: Ribonuclease a. Chain: a. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Cell_line: s2. Organ: pancreas
Resolution:
2.00Å     R-factor:   0.184    
Authors: P.C.Weber,S.Sheriff,D.H.Ohlendorf,B.C.Finzel,F.R.Salemme
Key ref: P.C.Weber et al. (1985). The 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41. Proc Natl Acad Sci U S A, 82, 8473-8477. PubMed id: 3936036 DOI: 10.1073/pnas.82.24.8473
Date:
27-Aug-85     Release date:   21-Jan-86    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 Enzyme reactions 
   Enzyme class: E.C.3.1.27.5  - 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!
  Cellular component     extracellular region   1 term 
  Biological process     metabolic process   3 terms 
  Biochemical function     nucleic acid binding     7 terms  

 

 
DOI no: 10.1073/pnas.82.24.8473 Proc Natl Acad Sci U S A 82:8473-8477 (1985)
PubMed id: 3936036  
 
 
The 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41.
P.C.Weber, S.Sheriff, D.H.Ohlendorf, B.C.Finzel, F.R.Salemme.
 
  ABSTRACT  
 
The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0-A resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  8142902 A.Kidera, K.Inaka, M.Matsushima, and N.Go (1994).
Response of dynamic structure to removal of a disulfide bond: normal mode refinement of C77A/C95A mutant of human lysozyme.
  Protein Sci, 3, 92.  
  7756988 I.Zegers, D.Maes, M.H.Dao-Thi, F.Poortmans, R.Palmer, and L.Wyns (1994).
The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules.
  Protein Sci, 3, 2322-2339.
PDB codes: 1rpf 1rpg 1rph
7986344 R.W.Dodge, J.H.Laity, D.M.Rothwarf, S.Shimotakahara, and H.A.Scheraga (1994).
Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A.
  J Protein Chem, 13, 409-421.  
1964787 M.Adler, and H.A.Scheraga (1990).
Identification of a new site of conformational heterogeneity in unfolded ribonuclease A.
  J Protein Chem, 9, 583-588.  
3449861 L.A.Svensson, L.Sjölin, G.L.Gilliland, B.C.Finzel, and A.Wlodawer (1986).
Multiple conformations of amino acid residues in ribonuclease A.
  Proteins, 1, 370-375.  
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.