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2khs

From Proteopedia

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[[Image:2khs.png|left|200px]]
 
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{{STRUCTURE_2khs| PDB=2khs | SCENE= }}
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==Solution structure of SNase121:SNase(111-143) complex==
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<StructureSection load='2khs' size='340' side='right'caption='[[2khs]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2khs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2KHS FirstGlance]. <br>
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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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2khs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khs OCA], [https://pdbe.org/2khs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2khs RCSB], [https://www.ebi.ac.uk/pdbsum/2khs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2khs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/2khs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2khs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 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.
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===Solution structure of SNase121:SNase(111-143) complex===
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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<ref>PMID:19658434</ref>
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{{ABSTRACT_PUBMED_19658434}}
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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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==About this Structure==
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<div class="pdbe-citations 2khs" style="background-color:#fffaf0;"></div>
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[[2khs]] is a 2 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=2KHS OCA].
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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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==Reference==
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<references/>
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<ref group="xtra">PMID:019658434</ref><references group="xtra"/>
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__TOC__
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[[Category: Micrococcal nuclease]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Feng, Y.]]
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[[Category: Feng Y]]
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[[Category: Geng, Y.]]
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[[Category: Geng Y]]
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[[Category: Shan, L.]]
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[[Category: Shan L]]
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[[Category: Wang, J.]]
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[[Category: Wang J]]
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[[Category: Xie, T.]]
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[[Category: Xie T]]
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[[Category: Endonuclease]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Nuclease]]
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[[Category: Secreted]]
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[[Category: Zymogen]]
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Current revision

Solution structure of SNase121:SNase(111-143) complex

PDB ID 2khs

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