1cpm
From Proteopedia
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|PDB= 1cpm |SIZE=350|CAPTION= <scene name='initialview01'>1cpm</scene>, resolution 2.0Å | |PDB= 1cpm |SIZE=350|CAPTION= <scene name='initialview01'>1cpm</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cpm OCA], [http://www.ebi.ac.uk/pdbsum/1cpm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cpm RCSB]</span> | ||
}} | }} | ||
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[[Category: Hahn, M.]] | [[Category: Hahn, M.]] | ||
[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
| - | [[Category: CA]] | ||
[[Category: hydrolase(glucanase)]] | [[Category: hydrolase(glucanase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:26:05 2008'' |
Revision as of 16:26, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Licheninase, with EC number 3.2.1.73 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS
Overview
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.
About this Structure
1CPM is a Single protein structure of sequence from Paenibacillus macerans. Full crystallographic information is available from OCA.
Reference
Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis., Hahn M, Piotukh K, Borriss R, Heinemann U, Proc Natl Acad Sci U S A. 1994 Oct 25;91(22):10417-21. PMID:7937966
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