2m00: Difference between revisions
m Protected "2m00" [edit=sysop:move=sysop] |
No edit summary |
||
| (9 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Solution structure of staphylococcal nuclease E43S mutant in the presence of ssDNA and Cd2+== | |||
<StructureSection load='2m00' size='340' side='right'caption='[[2m00]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2m00]] 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=2M00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M00 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2m00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m00 OCA], [https://pdbe.org/2m00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m00 RCSB], [https://www.ebi.ac.uk/pdbsum/2m00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m00 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Staphylococcal nuclease (SNase) catalyzes the hydrolysis of the phosphate backbone of DNA and RNA leaving 3'-phosphate mononucleotides and dinucleotides. SNase has been extensively used as a model protein for investigating enzymatic mechanism, thermodynamic stability, and protein folding. An unanswered question regarding enzymatic structure-function relationship is how SNase is capable of binding DNA and catalyzing the DNA hydrolysis. For understanding the mechanism of SNase-DNA interaction at the structural level, we have investigated the interactions between the E43S-mutant SNase ([E43S]SNase) and ssDNA in the presence of Cd(2+) using various NMR techniques including pulsed field gradient diffusion measurement, NMR titration and affinity measurement, chemical shift mapping, backbone dynamics, and three dimensional structural determination. [E43S]SNase retains the similar DNA-binding ability to the native SNase but loses its catalytic activity, and binding of ssDNA/Cd(2+) to [E43S]SNase induced certain degree backbone conformational exchange motion in the ssDNA and Cd(2+) binding regions, which might account for the preferential binding of DNA. Based on the NMR-derived structure of ssDNA/Cd(2+)-bound [E43S]SNase, we have built a three-dimensional model of the [E43S]SNase-ssDNA-Cd(2+) complex. The resulting model enabled the functional roles of SNase to be discussed, in particular the action of nuclease on ssDNA. | |||
Modeling of the [E43S]SNase-ssDNA-Cd(2+) complex: Structural insight into the action of nuclease on ssDNA.,Xie T, Feng Y, Shan L, Wang J Arch Biochem Biophys. 2013 Feb 14. pii: S0003-9861(13)00038-6. doi:, 10.1016/j.abb.2013.02.003. PMID:23416741<ref>PMID:23416741</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2m00" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus subsp. aureus MW2]] | |||
[[Category: Feng Y]] | |||
[[Category: Shan L]] | |||
[[Category: Wang J]] | |||
[[Category: Xie T]] | |||