First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.


From Proteopedia

Jump to: navigation, search

1clh, 12 NMR models ()
Gene: CYCLOPHILIN (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Publication Abstract from PubMed

The solution structure of the periplasmic cyclophilin type cis-trans peptidyl-prolyl isomerase from Escherichia coli (167 residues, MW > 18.200) has been determined using multidimensional heteronuclear NMR spectroscopy and distance geometry calculations. The structure determination is based on a total of 1720 NMR-derived restraints (1566 distance and 101 phi and 53 chi 1 torsion angle restraints). Twelve distance geometry structures were calculated, and the average root-mean-square (rms) deviation about the mean backbone coordinate positions is 0.84 +/- 0.18 A for the backbone atoms of residues 5-165 of the ensemble. The three-dimensional structure of E. coli cyclophilin consists of an eight-stranded antiparallel beta-sheet barrel capped by alpha-helices. The average coordinates of the backbone atoms of the core residues of E. coli cyclophilin have an rms deviation of 1.44 A, with conserved regions in the crystal structure of unligated human T cell cyclophilin [Ke, H. (1992) J. Mol. Biol. 228, 539-550]. Four regions proximal to the active site differ substantially and may determine protein substrate specificity, sensitivity to cyclosporin A, and the composite drug:protein surface required to inhibit calcineurin. A residue essential for isomerase activity in human T cell cyclophilin (His126) is replaced by Tyr122 in E. coli cyclophilin without affecting enzymatic activity.

Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin., Clubb RT, Ferguson SB, Walsh CT, Wagner G, Biochemistry. 1994 Mar 15;33(10):2761-72. PMID:8130188

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1clh is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA.

See Also


  • Clubb RT, Ferguson SB, Walsh CT, Wagner G. Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin. Biochemistry. 1994 Mar 15;33(10):2761-72. PMID:8130188

Proteopedia Page Contributors and Editors (what is this?)


Personal tools