3njn
From Proteopedia
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| - | [[ | + | ==Q118A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis== |
| + | <StructureSection load='3njn' size='340' side='right' caption='[[3njn]], [[Resolution|resolution]] 1.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3njn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Shewanella_oneidensis Shewanella oneidensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NJN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n55|3n55]], [[3njf|3njf]], [[3njg|3njg]], [[3njh|3njh]], [[3nji|3nji]], [[3njj|3njj]], [[3njk|3njk]], [[3njl|3njl]], [[3njm|3njm]]</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 Shewanella oneidensis])</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=3njn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3njn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3njn RCSB], [http://www.ebi.ac.uk/pdbsum/3njn PDBsum]</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/nj/3njn_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/chain_selection.php?pdb_ID=2ata 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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Shewanella oneidensis]] | [[Category: Shewanella oneidensis]] | ||
| - | [[Category: Bargassa, M | + | [[Category: Bargassa, M]] |
| - | [[Category: Collart, F | + | [[Category: Collart, F]] |
| - | [[Category: Joachimiak, A | + | [[Category: Joachimiak, A]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Mulligan, R | + | [[Category: Mulligan, R]] |
| - | [[Category: Osipiuk, J | + | [[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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Revision as of 11:06, 9 December 2014
Q118A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis
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