5sxy

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==The solution NMR structure for the PqqD truncation of Methylobacterium extorquens PqqCD representing a functional and stand-alone ribosomally synthesized and post-translational modified (RiPP) recognition element (RRE)==
==The solution NMR structure for the PqqD truncation of Methylobacterium extorquens PqqCD representing a functional and stand-alone ribosomally synthesized and post-translational modified (RiPP) recognition element (RRE)==
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<StructureSection load='5sxy' size='340' side='right' caption='[[5sxy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='5sxy' size='340' side='right'caption='[[5sxy]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5sxy]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SXY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5sxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens_AM1 Methylorubrum extorquens AM1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SXY FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyrroloquinoline-quinone_synthase Pyrroloquinoline-quinone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.11 1.3.3.11] </span></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</td></tr>
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<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=5sxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sxy OCA], [http://pdbe.org/5sxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sxy RCSB], [http://www.ebi.ac.uk/pdbsum/5sxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sxy ProSAT]</span></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=5sxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sxy OCA], [https://pdbe.org/5sxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sxy RCSB], [https://www.ebi.ac.uk/pdbsum/5sxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sxy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PQQCD_METEA PQQCD_METEA]] Ring cyclization and eight-electron oxidation of 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic-acid to PQQ.
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[https://www.uniprot.org/uniprot/PQQCD_METEA PQQCD_METEA] Ring cyclization and eight-electron oxidation of 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic-acid to PQQ.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), pyrroloquinoline quinone (PQQ), is initiated when the precursor peptide, PqqA, is recognized and bound by the RiPP precursor peptide recognition element (RRE), PqqD, for presentation to the first enzyme in the pathway, PqqE. Unlike other RiPP-producing, postribosomal peptide synthesis (PRPS) pathways in which the RRE is a component domain of the first enzyme, PqqD is predominantly a separate scaffolding protein that forms a ternary complex with the precursor peptide and first tailoring enzyme. As PqqD is a stable, independent RRE, this makes the PQQ pathway an ideal PRPS model system for probing RRE interactions using nuclear magnetic resonance (NMR). Herein, we present both the solution NMR structure of Methylobacterium extorquens PqqD and results of 1H-15N HSQC binding experiments that identify the PqqD residues involved in binding the precursor peptide, PqqA, and the enzyme, PqqE. The reported structural model for an independent RRE, along with the mapped binding surfaces, will inform future efforts both to understand and to manipulate PRPS pathways.
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Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone.,Evans RL 3rd, Latham JA, Xia Y, Klinman JP, Wilmot CM Biochemistry. 2017 May 12. doi: 10.1021/acs.biochem.7b00247. PMID:28481092<ref>PMID:28481092</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 5sxy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pyrroloquinoline-quinone synthase]]
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[[Category: Large Structures]]
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[[Category: Evans, R L]]
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[[Category: Methylorubrum extorquens AM1]]
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[[Category: Wilmot, C M]]
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[[Category: Evans RL]]
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[[Category: Xia, Y]]
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[[Category: Wilmot CM]]
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[[Category: Chaperone]]
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[[Category: Xia Y]]
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[[Category: Ripp rre peptide scaffolding]]
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Current revision

The solution NMR structure for the PqqD truncation of Methylobacterium extorquens PqqCD representing a functional and stand-alone ribosomally synthesized and post-translational modified (RiPP) recognition element (RRE)

PDB ID 5sxy

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