PDBsum entry 1rot

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Rotamase (isomerase) PDB id
Protein chain
118 a.a. *
* Residue conservation analysis
PDB id:
Name: Rotamase (isomerase)
Title: Structure of fkbp59-i, the n-terminal domain of a 59 kda fk506-binding protein, nmr, minimized average structure
Structure: Fkbp59-i. Chain: a. Synonym: fkbp52 or hsp56. Engineered: yes
Source: Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Organ: liver. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 1 models
Authors: C.T.Craescu,N.Rouviere,A.Popescu,E.Cerpolini,M.-C.Lebeau,E.- E.Baulieu,J.Mispelter
Key ref:
C.T.Craescu et al. (1996). Three-dimensional structure of the immunophilin-like domain of FKBP59 in solution. Biochemistry, 35, 11045-11052. PubMed id: 8780506 DOI: 10.1021/bi960975p
14-Jun-96     Release date:   07-Dec-96    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P27124  (FKBP4_RABIT) -  Peptidyl-prolyl cis-trans isomerase FKBP4
458 a.a.
118 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein folding   1 term 


    Added reference    
DOI no: 10.1021/bi960975p Biochemistry 35:11045-11052 (1996)
PubMed id: 8780506  
Three-dimensional structure of the immunophilin-like domain of FKBP59 in solution.
C.T.Craescu, N.Rouvière, A.Popescu, E.Cerpolini, M.C.Lebeau, E.E.Baulieu, J.Mispelter.
FKBP59 is a protein usually associated with heat-shock protein hsp90 and steroid receptors. The N-terminal domain of the rabbit liver protein (149 amino acids) has a sequence homology with FKBP12, binds FK506 immunosuppressor, and has a peptidyl-prolyl cis-trans isomerase activity. The three-dimensional structure of this domain (FKBP59-I) was determined using homo- and heteronuclear multidimensional NMR spectroscopy, distance geometry, and molecular dynamics methods. Structure calculations used 1290 interproton distance restraints derived from nuclear Overhauser enhancement measurements, 29 dihedral phi angle restraints, and 92 hydrogen bond restraints. For the final 22 structures, the root mean square distance from the mean atomic coordinates, calculated for well-defined secondary structure fragments, is 0.47 +/- 0.05 and 1.26 +/- 0.15 A for backbone heavy atoms (N, C alpha, C') and for all non-hydrogen atoms, respectively. The global fold contains a twisted six-stranded antiparallel beta-sheet and a short alpha-helix packed on the hydrophobic side of the sheet. The 20 N-terminal and 12 C-terminal amino acids of the domain are disordered. The main-chain structure of FKBP59-I is globally similar to the NMR-derived and X-ray structures of unbound FKBP12. An unusual hydrogen bond interaction between the indole amino proton of Trp 89 and the aromatic cycle of Phe 129 was observed. This gives a large upfield shift (-4.8 ppm) and a significant exchange protection factor. The implications of the present structure determination on the ligand binding of FKBP59 are discussed.

Literature references that cite this PDB file's key reference

  PubMed id Reference
14565867 N.Massol, M.C.Lebeau, M.Schumacher, and E.E.Baulieu (2003).
Promoter activity and gene structure of rabbit FKBP52.
  DNA Cell Biol, 22, 505-511.  
12116403 K.Kahn, and T.C.Bruice (2002).
Parameterization of OPLS-AA force field for the conformational analysis of macrocyclic polyketides.
  J Comput Chem, 23, 977-996.  
11751578 P.J.Pereira, M.C.Vega, E.González-Rey, R.Fernández-Carazo, S.Macedo-Ribeiro, F.X.Gomis-Rüth, A.González, and M.Coll (2002).
Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed alpha-helix.
  EMBO Rep, 3, 88-94.
PDB code: 1jvw
12454489 P.Li, C.Shu, B.Wu, Y.Ding, B.Shen, and Z.Rao (2002).
Crystallization and preliminary X-ray diffraction analysis of FKBP52 N-terminal domain.
  Acta Crystallogr D Biol Crystallogr, 58, 2168-2169.  
12045568 T.M.Myckatyn, R.A.Ellis, A.G.Grand, S.K.Sen, J.B.Lowe, D.A.Hunter, and S.E.Mackinnon (2002).
The effects of rapamycin in murine peripheral nerve isografts and allografts.
  Plast Reconstr Surg, 109, 2405-2417.  
11514681 A.Korepanova, C.Douglas, I.Leyngold, and T.M.Logan (2001).
N-terminal extension changes the folding mechanism of the FK506-binding protein.
  Protein Sci, 10, 1905-1910.  
11524681 A.Riboldi-Tunnicliffe, B.König, S.Jessen, M.S.Weiss, J.Rahfeld, J.Hacker, G.Fischer, and R.Hilgenfeld (2001).
Crystal structure of Mip, a prolylisomerase from Legionella pneumophila.
  Nat Struct Biol, 8, 779-783.
PDB code: 1fd9
10931176 A.Galat (2000).
Sequence diversification of the FK506-binding proteins in several different genomes.
  Eur J Biochem, 267, 4945-4959.  
10951192 C.Sich, S.Improta, D.J.Cowley, C.Guenet, J.P.Merly, M.Teufel, and V.Saudek (2000).
Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics.
  Eur J Biochem, 267, 5342-5355.
PDB code: 1f40
11058892 M.T.Ivery (2000).
Immunophilins: switched on protein binding domains?
  Med Res Rev, 20, 452-484.  
10051553 J.Clardy (1999).
Borrowing to make ends meet.
  Proc Natl Acad Sci U S A, 96, 1826-1827.  
10382674 M.Gastmans, G.Volckaert, and Y.Engelborghs (1999).
Tryptophan microstate reshuffling upon the binding of cyclosporin A to human cyclophilin A.
  Proteins, 35, 464-474.  
10051576 R.Briesewitz, G.T.Ray, T.J.Wandless, and G.R.Crabtree (1999).
Affinity modulation of small-molecule ligands by borrowing endogenous protein surfaces.
  Proc Natl Acad Sci U S A, 96, 1953-1958.  
  9385640 J.J.Prompers, A.Groenewegen, R.C.Van Schaik, H.A.Pepermans, and C.W.Hilbers (1997).
1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution.
  Protein Sci, 6, 2375-2384.  
9200682 N.Rouviere, M.Vincent, C.T.Craescu, and J.Gallay (1997).
Immunosuppressor binding to the immunophilin FKBP59 affects the local structural dynamics of a surface beta-strand: time-resolved fluorescence study.
  Biochemistry, 36, 7339-7352.  
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.