1clh
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(New page: 200px<br /><applet load="1clh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1clh" /> '''THREE-DIMENSIONAL SOLUTION STRUCTURE OF ESCH...)
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Revision as of 10:26, 20 November 2007
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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
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