1ihz
From Proteopedia
(New page: 200px<br /><applet load="1ihz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihz, resolution 1.65Å" /> '''Structure of S. nucl...) |
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| - | [[Image:1ihz.jpg|left|200px]]<br /><applet load="1ihz" size=" | + | [[Image:1ihz.jpg|left|200px]]<br /><applet load="1ihz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ihz, resolution 1.65Å" /> | caption="1ihz, resolution 1.65Å" /> | ||
'''Structure of S. nuclease mutant quintuple mutant V23L/V66L/I72L/I92L/V99L'''<br /> | '''Structure of S. nuclease mutant quintuple mutant V23L/V66L/I72L/I92L/V99L'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Efforts to design proteins with greatly reduced sequence diversity have | + | 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== | ==About this Structure== | ||
| - | 1IHZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [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] Full crystallographic information is available from [http:// | + | 1IHZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lu, Z.]] | [[Category: Lu, Z.]] | ||
[[Category: Sakon, J.]] | [[Category: Sakon, J.]] | ||
| - | [[Category: Stites, W | + | [[Category: Stites, W E.]] |
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:03 2008'' |
Revision as of 11:12, 21 February 2008
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Structure of S. nuclease mutant quintuple mutant V23L/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
1IHZ is a Single protein structure of sequence from Staphylococcus aureus. Active as Micrococcal nuclease, with EC number 3.1.31.1 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
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