1ii3

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[[Image:1ii3.gif|left|200px]]
[[Image:1ii3.gif|left|200px]]
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{{Structure
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|PDB= 1ii3 |SIZE=350|CAPTION= <scene name='initialview01'>1ii3</scene>, resolution 1.72&Aring;
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The line below this paragraph, containing "STRUCTURE_1ii3", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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{{STRUCTURE_1ii3| PDB=1ii3 | SCENE= }}
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|RELATEDENTRY=[[1ey0|1EY0]], [[1ihz|1IHZ]]
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1ii3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ii3 RCSB]</span>
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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'''
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[[Category: Sakon, J.]]
[[Category: Sakon, J.]]
[[Category: Stites, W E.]]
[[Category: Stites, W E.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:01:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:06 2008''
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Revision as of 17:01, 2 May 2008

Template:STRUCTURE 1ii3

Structure of S. nuclease quintuple mutant V23I/V66L/I72L/I92L/V99L


Overview

Efforts 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.

About this Structure

1II3 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 20:01:36 2008

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