2khs: Difference between revisions
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<StructureSection load='2khs' size='340' side='right' caption='[[2khs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2khs' size='340' side='right' caption='[[2khs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2khs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2khs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KHS FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nuc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nuc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2khs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2khs RCSB], [http://www.ebi.ac.uk/pdbsum/2khs PDBsum]</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=2khs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khs OCA], [http://pdbe.org/2khs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2khs RCSB], [http://www.ebi.ac.uk/pdbsum/2khs PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2khs" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Micrococcal nuclease]] | [[Category: Micrococcal nuclease]] | ||
[[Category: Feng, Y]] | [[Category: Feng, Y]] | ||
[[Category: Geng, Y]] | [[Category: Geng, Y]] | ||
Revision as of 05:53, 11 September 2015
Solution structure of SNase121:SNase(111-143) complexSolution structure of SNase121:SNase(111-143) complex
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 PubMedThe interactions necessary for stabilizing the folding of the N-terminal large beta-subdomain and the C-terminal small alpha-subdomain of staphylococcal nuclease (SNase) were investigated by an approach of fragment complementation. Two SNase fragments, namely, SNase121 and SNase(111-143) containing 1-121 and 111-143 residues, respectively, of native SNase, were used in this study since the sequences of the two fragments correspond to that of the beta- and alpha-subdomains of SNase. SNase121 is a largely unfolded fragment whereas SNase(111-143) is a structureless fragment. The recognition process and efficiency of complementation of SNase121 and SNase(111-143) fragments were studied by NMR and various biochemical and biophysical methods. SNase121 and SNase(111-143) can recognize each other and recover their native conformations on binding, restoring the active site and the ability to degrade DNA. The SNase121:SNase(111-143) complex showed a nuclease activity up to 30% that of native SNase. The final rigid structures of SNase121 and SNase(111-143) fragments having the folded native-like beta-subdomain and alpha-subdomain structures of SNase, respectively, in the complex form simultaneously with the complex stabilization. Studies with the mutant SNase121 and SNase(111-143) fragments reveal that the sequence elements which are essential for recognition and efficient complementation of the two fragments are also necessary for recovering the native-like interactions at the binding interface between them. The interfragment interactions that induce the structural complementation of SNase121 and SNase(111-143) likely reflect the tertiary interactions necessary to stabilize the folding of both beta- and alpha-subdomains in the native SNase. The native-like interactions between SNase121 and SNase(111-143) fragments induce the recovery of their native-like structures and the ability to degrade DNA.,Geng Y, Feng Y, Xie T, Shan L, Wang J Biochemistry. 2009 Sep 15;48(36):8692-703. PMID:19658434[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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