1ii3: Difference between revisions
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==Structure of S. nuclease quintuple mutant V23I/V66L/I72L/I92L/V99L== | ==Structure of S. nuclease quintuple mutant V23I/V66L/I72L/I92L/V99L== | ||
<StructureSection load='1ii3' size='340' side='right' caption='[[1ii3]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='1ii3' size='340' side='right' caption='[[1ii3]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ey0|1ey0]], [[1ihz|1ihz]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ey0|1ey0]], [[1ihz|1ihz]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] </span></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=1ii3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii3 OCA], [http://pdbe.org/1ii3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ii3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ii3 PDBsum]</span></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=1ii3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii3 OCA], [http://pdbe.org/1ii3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ii3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ii3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ii3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ii/1ii3_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ii/1ii3_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1ii3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1ii3" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:28, 10 January 2018
Structure of S. nuclease quintuple mutant V23I/V66L/I72L/I92L/V99LStructure of S. nuclease quintuple mutant V23I/V66L/I72L/I92L/V99L
Structural highlights
Function[NUC_STAAU] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEfforts to design proteins with greatly reduced sequence diversity have often resulted in proteins with so-called molten globule properties. Substitutions were made at six neighboring sites in the major hydrophobic core of staphylococcal nuclease to create variants with all leucine, all isoleucine or all valine at these sites. The mutant proteins with simplified cores constructed here are quite unstable and have poorly packed cores, attested to by interaction energies. Eight related mutants with greater sequence diversity were also constructed. Comparison to these mutants and 159 other permutations of these 3 aliphatic side chains at these same 6 sites previously constructed shows that the simplified cores are not unusual in their stabilities or interaction energies. Further, crystal structures of the two mutants with the worst packing, as measured by interaction energies, showed no unusual disorder in the core. Therefore, reduction of sequence diversity is not necessarily incompatible with a single stable native structure. Other factors must also contribute to previous protein design failures. Proteins with simplified hydrophobic cores compared to other packing mutants.,Chen J, Lu Z, Sakon J, Stites WE Biophys Chem. 2004 Aug 1;110(3):239-48. PMID:15228960[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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