2pqe

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(New page: 200px<br /><applet load="2pqe" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pqe" /> '''Solution structure of proline-free mutant of...)
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[[Image:2pqe.gif|left|200px]]<br /><applet load="2pqe" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2pqe" />
 
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'''Solution structure of proline-free mutant of staphylococcal nuclease'''<br />
 
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==Overview==
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==Solution structure of proline-free mutant of staphylococcal nuclease==
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The role of cis-trans isomerizations of peptidyl-proline bonds in the, enzyme activity of staphylococcal nuclease (SNase) was examined by, mutation of proline residues. The proline-free SNase ([Pro-]SNase), namely, P11A/P31A/P42A/P47T/P56A/P117G-mutant SNase, was adopted for, elucidating the correlation between the nuclease activity and the backbone, conformational and dynamic states of SNase. The 3D solution structure of, [Pro-]SNase has been determined by heteronuclear NMR experiments., Comparing the structure of [Pro-]SNase with the structure of SNase, revealed the conformational differences between the two proteins. In the, structure of [Pro-]SNase, conformational rearrangements were observed for, the loop of residues Ala112-His121 containing a trans Lys116-Gly117, peptide bond and for the C-terminal alpha-helical loop of residues, Leu137-Glu142. Mutation of proline at position 117 also caused the, conformational rearrangement of the p-loop (Asp77-Leu89), which is remote, from the Ala112-His121 loop. The Ala112-His121 loop and p-loop are placed, closer to each other in [Pro-]SNase than in SNase. The backbone dynamic, features of the omega-loop (Pro42-Pro56) of SNase are different from those, of [Pro-]SNase. The backbone of the omega-loop exhibits restricted, flexibility with slow conformational exchange motions in SNase, but is, highly flexible in [Pro-]SNase. The analysis indicates that the restrained, backbone conformation of the Ala112-His121 loop and restricted flexibility, of the omega-loop are two dominant factors determining the enzyme activity, of SNase. Of the two factors, the former is correlated with the strained, cis Lys116-Pro117 peptide bond and the latter is correlated with the, cis-trans isomerizations of the His46-Pro47 peptide bond.
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<StructureSection load='2pqe' size='340' side='right'caption='[[2pqe]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2pqe]] is a 1 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=2PQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQE 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=2pqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqe OCA], [https://pdbe.org/2pqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqe RCSB], [https://www.ebi.ac.uk/pdbsum/2pqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqe 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/pq/2pqe_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=2pqe 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 role of cis-trans isomerizations of peptidyl-proline bonds in the enzyme activity of staphylococcal nuclease (SNase) was examined by mutation of proline residues. The proline-free SNase ([Pro-]SNase), namely, P11A/P31A/P42A/P47T/P56A/P117G-mutant SNase, was adopted for elucidating the correlation between the nuclease activity and the backbone conformational and dynamic states of SNase. The 3D solution structure of [Pro-]SNase has been determined by heteronuclear NMR experiments. Comparing the structure of [Pro-]SNase with the structure of SNase revealed the conformational differences between the two proteins. In the structure of [Pro-]SNase, conformational rearrangements were observed for the loop of residues Ala112-His121 containing a trans Lys116-Gly117 peptide bond and for the C-terminal alpha-helical loop of residues Leu137-Glu142. Mutation of proline at position 117 also caused the conformational rearrangement of the p-loop (Asp77-Leu89), which is remote from the Ala112-His121 loop. The Ala112-His121 loop and p-loop are placed closer to each other in [Pro-]SNase than in SNase. The backbone dynamic features of the omega-loop (Pro42-Pro56) of SNase are different from those of [Pro-]SNase. The backbone of the omega-loop exhibits restricted flexibility with slow conformational exchange motions in SNase, but is highly flexible in [Pro-]SNase. The analysis indicates that the restrained backbone conformation of the Ala112-His121 loop and restricted flexibility of the omega-loop are two dominant factors determining the enzyme activity of SNase. Of the two factors, the former is correlated with the strained cis Lys116-Pro117 peptide bond and the latter is correlated with the cis-trans isomerizations of the His46-Pro47 peptide bond.
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==About this Structure==
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Restricted backbone conformational and motional flexibilities of loops containing peptidyl-proline bonds dominate the enzyme activity of staphylococcal nuclease.,Shan L, Tong Y, Xie T, Wang M, Wang J Biochemistry. 2007 Oct 16;46(41):11504-13. Epub 2007 Sep 22. PMID:17887731<ref>PMID:17887731</ref>
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2PQE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQE OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Restricted backbone conformational and motional flexibilities of loops containing peptidyl-proline bonds dominate the enzyme activity of staphylococcal nuclease., Shan L, Tong Y, Xie T, Wang M, Wang J, Biochemistry. 2007 Oct 16;46(41):11504-13. Epub 2007 Sep 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17887731 17887731]
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</div>
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[[Category: Micrococcal nuclease]]
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<div class="pdbe-citations 2pqe" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
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[[Category: Shan, L.]]
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[[Category: Tong, Y.]]
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[[Category: Wang, J.]]
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[[Category: Wang, M.]]
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[[Category: Xie, T.]]
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[[Category: beta barrel]]
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[[Category: hydrolase]]
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[[Category: ob fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:19:55 2008''
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==See Also==
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*[[Staphylococcal nuclease 3D structures|Staphylococcal nuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Staphylococcus aureus]]
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[[Category: Shan L]]
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[[Category: Tong Y]]
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[[Category: Wang J]]
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[[Category: Wang M]]
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[[Category: Xie T]]

Current revision

Solution structure of proline-free mutant of staphylococcal nuclease

PDB ID 2pqe

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