1cpm: Difference between revisions

Line 1:

[[Image:1cpm.gif|left|200px]]<br /><applet load="1cpm" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1cpm.gif|left|200px]]<br /><applet load="1cpm" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1cpm, resolution 2.0Å" />

'''NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1CPM OCA].

1CPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPM OCA].

==Reference==

Line 19:

[[Category: hydrolase(glucanase)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 12:39:~~13 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:27 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1cpm.gif|left|200px]]<br /><applet load="1cpm" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cpm.gif|left|200px]]<br /><applet load="1cpm" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cpm, resolution 2.0&Aring;" />
 '''NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS'''<br />
 ==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.
+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==
-CPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CPM OCA].
+CPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPM OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: hydrolase(glucanase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:39:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:27 2008''