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1ey5

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[[Image:1ey5.gif|left|200px]]
 
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==STRUCTURE OF S. NUCLEASE STABILIZING MUTANT T33V==
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The line below this paragraph, containing "STRUCTURE_1ey5", creates the "Structure Box" on the page.
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<StructureSection load='1ey5' size='340' side='right'caption='[[1ey5]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ey5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EY5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ey5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ey5 OCA], [https://pdbe.org/1ey5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ey5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ey5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ey5 ProSAT]</span></td></tr>
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{{STRUCTURE_1ey5| PDB=1ey5 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NUC_STAAU NUC_STAAU] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/1ey5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ey5 ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF S. NUCLEASE STABILIZING MUTANT T33V'''
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==See Also==
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*[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Seven hyper-stable multiple mutants have been constructed in staphylococcal nuclease by various combinations of eight different stabilizing single mutants. The stabilities of these multiple mutants determined by guanidine hydrochloride denaturation were 3.4 to 5.6 kcal/mol higher than that of the wild-type. Their thermal denaturation midpoint temperatures were 12.6 to 22.9 deg. C higher than that of the wild-type. These are among the greatest increases in protein stability and thermal denaturation midpoint temperature relative to the wild-type yet attained. There has been great interest in understanding how proteins found in thermophilic organisms are stabilized. One frequently cited theory is that the packing of hydrophobic side-chains is improved in the cores of proteins isolated from thermophiles when compared to proteins from mesophiles. The crystal structures of four single and five multiple stabilizing mutants of staphylococcal nuclease were solved to high resolution. No large overall structural change was found, with most changes localized around the sites of mutation. Rearrangements were observed in the packing of side-chains in the major hydrophobic core, although none of the mutations was in the core. It is surprising that detailed structural analysis showed that packing had improved, with the volume of the mutant protein's hydrophobic cores decreasing as protein stability increased. Further, the number of van der Waals interactions in the entire protein showed an experimentally significant increase correlated with increasing stability. These results indicate that optimization of packing follows as a natural consequence of increased protein thermostability and that good packing is not necessarily the proximate cause of high stability. Another popular theory is that thermostable proteins have more electrostatic and hydrogen bonding interactions and these are responsible for the high stabilities. The mutants here show that increased numbers of electrostatic and hydrogen bonding interactions are not obligatory for large increases in protein stability.
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[[Category: Large Structures]]
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==About this Structure==
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1EY5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EY5 OCA].
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==Reference==
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Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability., Chen J, Lu Z, Sakon J, Stites WE, J Mol Biol. 2000 Oct 20;303(2):125-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11023780 11023780]
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[[Category: Micrococcal nuclease]]
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Chen, J.]]
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[[Category: Chen J]]
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[[Category: Lu, Z.]]
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[[Category: Lu Z]]
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[[Category: Sakon, J.]]
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[[Category: Sakon J]]
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[[Category: Stites, W E.]]
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[[Category: Stites WE]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:39:45 2008''
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Current revision

STRUCTURE OF S. NUCLEASE STABILIZING MUTANT T33V

PDB ID 1ey5

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