1clh
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1clh.gif|left|200px]] | + | [[Image:1clh.gif|left|200px]] |
| - | + | ||
| - | '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF ESCHERICHIA COLI PERIPLASMIC CYCLOPHILIN''' | + | {{Structure |
| + | |PDB= 1clh |SIZE=350|CAPTION= <scene name='initialview01'>1clh</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF ESCHERICHIA COLI PERIPLASMIC CYCLOPHILIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1CLH is a [ | + | 1CLH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLH OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8130188 8130188] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 17: | Line 26: | ||
[[Category: isomerase(peptidyl-prolyl cis-trans)]] | [[Category: isomerase(peptidyl-prolyl cis-trans)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:55 2008'' |
Revision as of 08:25, 20 March 2008
| |||||||
| Gene: | CYCLOPHILIN (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE-DIMENSIONAL SOLUTION STRUCTURE OF ESCHERICHIA COLI PERIPLASMIC CYCLOPHILIN
Overview
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.
About this Structure
1CLH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 10:25:55 2008
