PDBsum entry 1cpm

Hydrolase(glucanase)

PDB id: 1cpm

Contents

Protein chain

214 a.a.

Metals

_CA

Waters ×125

References listed in PDB file

Key reference

• Title: Native-Like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis.
• Authors: M.Hahn, K.Piotukh, R.Borriss, U.Heinemann.
• Ref.: Proc Natl Acad Sci U S A, 1994, 91, 10417-10421. [DOI no: 10.1073/pnas.91.22.10417]
• PubMed id: 7937966

Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a perfect match.

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.

Secondary reference #1

• Title: Molecular and active-Site structure of a bacillus 1,3-1,4-Beta-Glucanase.
• Authors: T.Keitel, O.Simon, R.Borriss, U.Heinemann.
• Ref.: Proc Natl Acad Sci U S A, 1993, 90, 5287-5291. [DOI no: 10.1073/pnas.90.11.5287]
• PubMed id: 8099449