1cpm

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(New page: 200px<br /><applet load="1cpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cpm, resolution 2.0&Aring;" /> '''NATIVE-LIKE IN VIVO F...)
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[[Image:1cpm.gif|left|200px]]<br /><applet load="1cpm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cpm, resolution 2.0&Aring;" />
 
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'''NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS'''<br />
 
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==Overview==
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==NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS==
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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.
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<StructureSection load='1cpm' size='340' side='right'caption='[[1cpm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cpm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans]. The April 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Concanavalin A and Circular Permutation'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_4 10.2210/rcsb_pdb/mom_2010_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CPM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cpm OCA], [https://pdbe.org/1cpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cpm RCSB], [https://www.ebi.ac.uk/pdbsum/1cpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cpm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUB_PAEMA GUB_PAEMA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cp/1cpm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cpm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:7937966</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7937966 7937966]
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</div>
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[[Category: Licheninase]]
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<div class="pdbe-citations 1cpm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Concanavalin A and Circular Permutation]]
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[[Category: Large Structures]]
[[Category: Paenibacillus macerans]]
[[Category: Paenibacillus macerans]]
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[[Category: Single protein]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Hahn, M.]]
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[[Category: Hahn M]]
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[[Category: Heinemann, U.]]
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[[Category: Heinemann U]]
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[[Category: CA]]
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[[Category: hydrolase(glucanase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:39:13 2007''
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Current revision

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

PDB ID 1cpm

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