5nuc: Difference between revisions
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<StructureSection load='5nuc' size='340' side='right'caption='[[5nuc]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5nuc' size='340' side='right'caption='[[5nuc]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nuc]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5nuc]] 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=5NUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NUC FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <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=PEC:S,S-PENTYLTHIOCYSTEINE'>PEC</scene>, <scene name='pdbligand=THP:THYMIDINE-3,5-DIPHOSPHATE'>THP</scene></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=5nuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nuc OCA], [https://pdbe.org/5nuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nuc RCSB], [https://www.ebi.ac.uk/pdbsum/5nuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nuc ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: Fox | [[Category: Fox RO]] | ||
[[Category: Harkins | [[Category: Harkins PC]] | ||
[[Category: Richards | [[Category: Richards FM]] | ||
[[Category: Wynn | [[Category: Wynn R]] | ||
Latest revision as of 09:51, 9 August 2023
STAPHYLOCOCCAL NUCLEASE, 1-N-PENTANE THIOL DISULFIDE TO V23C VARIANTSTAPHYLOCOCCAL NUCLEASE, 1-N-PENTANE THIOL DISULFIDE TO V23C VARIANT
Structural highlights
FunctionNUC_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 PubMedThe 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 AlsoReferences
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