2m57

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2m57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M57 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2m57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M57 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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2m57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m57 OCA], [https://pdbe.org/2m57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m57 RCSB], [https://www.ebi.ac.uk/pdbsum/2m57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m57 ProSAT]</span></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=2m57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m57 OCA], [https://pdbe.org/2m57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m57 RCSB], [https://www.ebi.ac.uk/pdbsum/2m57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m57 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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NMR spectroscopy has revealed pH-dependent structural changes in the highly conserved catalytic domain 5 of a bacterial group II intron. Two adenines with pK(a) values close to neutral pH were identified in the catalytic triad and the bulge. Protonation of the adenine opposite to the catalytic triad is stabilized within a G(syn)-AH(+) (anti) base pair. The pH-dependent anti-to-syn flipping of this G in the catalytic triad modulates the known interaction with the linker region between domains 2 and 3 (J23) and simultaneously the binding of the catalytic Mg(2+) ion to its backbone. Hence, this here identified shifted pK(a) value controls the conformational change between the two steps of splicing.
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Protonation-Dependent Base Flipping at Neutral pH in the Catalytic Triad of a Self-Splicing Bacterial Group II Intron.,Pechlaner M, Donghi D, Zelenay V, Sigel RK Angew Chem Int Ed Engl. 2015 Aug 10;54(33):9687-90. doi: 10.1002/anie.201504014. , Epub 2015 Jun 26. PMID:26119804<ref>PMID:26119804</ref>
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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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<div class="pdbe-citations 2m57" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

NMR solution structure of domain 5 from Azotobacter vinelandii Intron 5 at pH 7.8

PDB ID 2m57

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