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2lkv

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==Staphylococcal Nuclease PHS variant==
==Staphylococcal Nuclease PHS variant==
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<StructureSection load='2lkv' size='340' side='right' caption='[[2lkv]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2lkv' size='340' side='right'caption='[[2lkv]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lkv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LKV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2lkv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKV FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nuc, MW0769 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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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=2lkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkv OCA], [https://pdbe.org/2lkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkv RCSB], [https://www.ebi.ac.uk/pdbsum/2lkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkv ProSAT]</span></td></tr>
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<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=2lkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lkv RCSB], [http://www.ebi.ac.uk/pdbsum/2lkv PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/NUC_STAAW NUC_STAAW] Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond (By similarity).
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Mannosylglycerate is a compatible solute typical of thermophilic marine microorganisms that has a remarkable ability to protect proteins from thermal denaturation. This ionic solute appears to be a universal stabilizing agent, but the extent of protection depends on the specific protein examined. To understand how mannosylglycerate confers protection, we have been studying its influence on the internal motions of a hyperstable staphylococcal nuclease (SNase). Previously, we found a correlation between the magnitude of protein stabilization and the restriction of fast backbone motions. We now report the effect of mannosylglycerate on the fast motions of side-chains and on the slower unfolding motions of the protein. Side-chain motions were assessed by (13) CH(3) relaxation measurements and model-free analysis while slower unfolding motions were probed by H/D exchange measurements at increasing concentrations of urea. Side-chain motions were little affected by the presence of different concentrations of mannosylglycerate or even by the presence of urea (0.25M), and show no correlation with changes in the thermodynamic stability of SNase. Native hydrogen exchange experiments showed that, contrary to reports on other stabilizing solutes, mannosylglycerate restricts local motions in addition to the global motions of the protein. The protein unfolding/folding pathway remained undisturbed in the presence of mannosylglycerate but the solute showed a specific effect on the local motions of beta-sheet residues. This work reinforces the link between solute-induced stabilization and restriction of protein motions at different timescales, and shows that the solute preferentially affects specific structural elements of SNase.
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Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow beta-sheet motions.,Pais TM, Lamosa P, Matzapetakis M, Turner DL, Santos H Protein Sci. 2012 Aug;21(8):1126-37. doi: 10.1002/pro.2100. Epub 2012 Jun 15. PMID:22619184<ref>PMID:22619184</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Staphylococcal nuclease|Staphylococcal nuclease]]
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*[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Micrococcal nuclease]]
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[[Category: Large Structures]]
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[[Category: Staphylococcus aureus]]
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[[Category: Staphylococcus aureus subsp. aureus MW2]]
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[[Category: Lamosa, P]]
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[[Category: Lamosa P]]
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[[Category: Matzapetakis, M]]
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[[Category: Matzapetakis M]]
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[[Category: Pais, T M]]
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[[Category: Pais TM]]
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[[Category: Santos, H]]
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[[Category: Santos H]]
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[[Category: Turner, D L]]
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[[Category: Turner DL]]
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[[Category: Hydrolase]]
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Current revision

Staphylococcal Nuclease PHS variant

PDB ID 2lkv

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