1CPM

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

Summary for 1CPM

• Entry DOI: 10.2210/pdb1cpm/pdb
• Descriptor: CIRCULARLY PERMUTED, CALCIUM ION (3 entities in total)
• Functional Keywords: hydrolase(glucanase)
• Biological source: Paenibacillus macerans
• Total number of polymer chains: 1
• Total formula weight: 23917.20

Authors

Hahn, M.,Heinemann, U. (deposition date: 1994-03-11, release date: 1994-06-22, Last modification date: 2024-10-30)

Primary citation

Hahn, M.,Piotukh, K.,Borriss, R.,Heinemann, U.
Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis.
Proc.Natl.Acad.Sci.USA, 91:10417-10421, 1994

PubMed Abstract: 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.

PubMed: 7937966
DOI: 10.1073/pnas.91.22.10417

Experimental method

X-RAY DIFFRACTION (2 Å)