1cpm: Difference between revisions

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[[Image:1cpm.gif|left|200px]]
{{Seed}}
[[Image:1cpm.png|left|200px]]


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{{STRUCTURE_1cpm|  PDB=1cpm  |  SCENE=  }}  
{{STRUCTURE_1cpm|  PDB=1cpm  |  SCENE=  }}  


'''NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS'''
===NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS===




==Overview==
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A jellyroll beta-sandwich protein, the Bacillus beta-glucanase H(A16-M), is used to probe the role of N-terminal peptide regions in protein folding in vivo. A gene encoding H(A16-M) is rearranged to place residues 1-58 of the protein behind a signal peptide and residues 59-214. The rearranged gene is expressed in Escherichia coli. The resultant circularly permuted protein, cpA16M-59, is secreted into the periplasm, correctly processed, and folded into a stable and active enzyme. Crystal structure analysis at 2.0-A resolution, R = 15.3%, shows cpA16M-59 to have a three-dimensional structure nearly identical with that of the parent beta-glucanase. An analogous experiment based on the wild-type Bacillus macerans beta-glucanase, giving rise to the circularly permuted variant cpMAC-57, yields the same results. Folding of these proteins, therefore, is not a vectorial process depending on the conformation adopted by their native N-terminal oligopeptides after ribosomal synthesis and translocation through the cytoplasmic membrane.
The line below this paragraph, {{ABSTRACT_PUBMED_7937966}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_7937966}}


==About this Structure==
==About this Structure==
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[[Category: Hahn, M.]]
[[Category: Hahn, M.]]
[[Category: Heinemann, U.]]
[[Category: Heinemann, U.]]
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