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3n55
From Proteopedia
(Difference between revisions)
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| - | [[Image:3n55.jpg|left|200px]] | ||
| - | < | + | ==SO1698 protein, an aspartic peptidase from Shewanella oneidensis.== |
| - | + | <StructureSection load='3n55' size='340' side='right' caption='[[3n55]], [[Resolution|resolution]] 1.57Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3n55]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700550 Atcc 700550]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ai4 2ai4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N55 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SO_1698 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70863 ATCC 700550])</td></tr> | |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n55 OCA], [http://pdbe.org/3n55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n55 RCSB], [http://www.ebi.ac.uk/pdbsum/3n55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n55 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/3n55_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3n55 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of SO1698 protein from Shewanella oneidensis was determined by a SAD method and refined to 1.57 A. The structure is a beta sandwich that unexpectedly consists of two polypeptides; the N-terminal fragment includes residues 1-116, and the C-terminal one includes residues 117-125. Electron density also displayed the Lys-98 side chain covalently linked to Asp-116. The putative active site residues involved in self-cleavage were identified; point mutants were produced and characterized structurally and in a biochemical assay. Numerical simulations utilizing molecular dynamics and hybrid quantum/classical calculations suggest a mechanism involving activation of a water molecule coordinated by a catalytic aspartic acid. | ||
| - | + | Characterization of member of DUF1888 protein family, self-cleaving and self-assembling endopeptidase.,Osipiuk J, Mulligan R, Bargassa M, Hamilton JE, Cunningham MA, Joachimiak A J Biol Chem. 2012 Jun 1;287(23):19452-61. Epub 2012 Apr 5. PMID:22493430<ref>PMID:22493430</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3n55" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: Collart, F | + | <references/> |
| - | [[Category: Joachimiak, A | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Mulligan, R | + | [[Category: Atcc 700550]] |
| - | [[Category: Osipiuk, J | + | [[Category: Collart, F]] |
| + | [[Category: Joachimiak, A]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Mulligan, R]] | ||
| + | [[Category: Osipiuk, J]] | ||
[[Category: Aspartic peptidase]] | [[Category: Aspartic peptidase]] | ||
[[Category: Autocatalysis]] | [[Category: Autocatalysis]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
| - | [[Category: | + | [[Category: PSI, Protein structure initiative]] |
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Current revision
SO1698 protein, an aspartic peptidase from Shewanella oneidensis.
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