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| | ==STAPHLOCOCCAL NUCLEASE, ETHANE THIOL DISULFIDE TO V23C VARIANT== | | ==STAPHLOCOCCAL NUCLEASE, ETHANE THIOL DISULFIDE TO V23C VARIANT== |
| - | <StructureSection load='2nuc' size='340' side='right' caption='[[2nuc]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2nuc' size='340' side='right'caption='[[2nuc]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nuc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NUC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nuc]] 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=2NUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NUC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=THP:THYMIDINE-3,5-DIPHOSPHATE'>THP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCS:3-(ETHYLDISULFANYL)-L-ALANINE'>SCS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SCS:3-(ETHYLDISULFANYL)-L-ALANINE'>SCS</scene>, <scene name='pdbligand=THP:THYMIDINE-3,5-DIPHOSPHATE'>THP</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2nuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nuc OCA], [https://pdbe.org/2nuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nuc RCSB], [https://www.ebi.ac.uk/pdbsum/2nuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nuc ProSAT]</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=2nuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nuc OCA], [http://pdbe.org/2nuc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nuc RCSB], [http://www.ebi.ac.uk/pdbsum/2nuc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nuc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Staphylococcal nuclease|Staphylococcal nuclease]] | + | *[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Micrococcal nuclease]] | + | [[Category: Large Structures]] |
| - | [[Category: Fox, R O]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Harkins, P C]] | + | [[Category: Fox RO]] |
| - | [[Category: Richards, F M]] | + | [[Category: Harkins PC]] |
| - | [[Category: Wynn, R]] | + | [[Category: Richards FM]] |
| - | [[Category: Endonuclease]] | + | [[Category: Wynn R]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nuclease]]
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| 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 PubMed
The structures of several variants of staphylococcal nuclease with long flexible unnatural amino acid side chains in the hydrophobic core have been determined by X-ray crystallography. The unnatural amino acids are disulfide moieties between the lone cysteine residue in V23C nuclease and methane, ethane, 1-n-propane, 1-n-butane, 1-n-pentane, and 2-hydroxyethyl thiols. We have examined changes in the core packing of these mutants. Side chains as large as the 1-n-propyl cysteine disulfide can be incorporated without perturbation of the structure. This is due, in part, to cavities present in the wild-type protein. The longest side chains are not well defined, even though they remain buried within the protein interior. These results suggest that the enthalpy-entropy balance that governs the rigidity of protein interiors favors tight packing only weakly. Additionally, the tight packing observed normally in protein interiors may reflect, in part, the limited numbers of rotamers available to the natural amino acids.
Mobile unnatural amino acid side chains in the core of staphylococcal nuclease.,Wynn R, Harkins PC, Richards FM, Fox RO Protein Sci. 1996 Jun;5(6):1026-31. PMID:8762134[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wynn R, Harkins PC, Richards FM, Fox RO. Mobile unnatural amino acid side chains in the core of staphylococcal nuclease. Protein Sci. 1996 Jun;5(6):1026-31. PMID:8762134 doi:http://dx.doi.org/10.1002/pro.5560050605
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