Secondary structure and backbone resonance assignments of the periplasmic cyclophilin type peptidyl-prolyl isomerase from Escherichia coli.
Proton, carbon-13, and nitrogen-15 sequence-specific backbone assignments have been obtained for the periplasmic cyclophilin type cis-trans peptidyl-prolyl isomerase from Escherichia coli (167 residues, M(r) = 18,244). Assignments were obtained using both 1H, 13C, and 15N triple-resonance and 1H and 15N double-resonance three-dimensional (3D) NMR spectroscopy at pH 6.2, 25 degrees C. Complete or partial residue-specific assignments have been obtained for 165 of the 167 residues. The secondary structure has been characterized using long- and medium-range NOEs. The protein consists of an eight-stranded anti-parallel beta-sheet and two helices. The overall topology of E. coli cyclophilin is similar to that of human T-cell cyclophilin. Sequence alignment with human T-cell cyclophilin based on secondary structure homology implicates several residues in E. coli cyclophilin that may be crucial for binding the peptide substrate AC-A-A-P-A-AMC and the immunosuppressive drug cyclosporin A.
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Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
Thanabal
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Fejzo
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Ferguson
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Zydowsky
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Baker
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Walsh
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Wagner
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D000591:Amino Acid Isomerases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D016572:Cyclosporine / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008961:Models, Structural; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D019696:Peptidylprolyl Isomerase; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D002352:Carrier Proteins; D009842:Oligopeptides; D011994:Recombinant Proteins; D016572:Cyclosporine; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase