9b1u

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Current revision (13:09, 21 August 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9b1u is ON HOLD until Paper Publication
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==Crystal structure of PqqT with PQQ bound==
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<StructureSection load='9b1u' size='340' side='right'caption='[[9b1u]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9b1u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens Methylorubrum extorquens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9B1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9B1U 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">X-ray diffraction, [[Resolution|Resolution]] 1.46&#8491;</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=9b1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9b1u OCA], [https://pdbe.org/9b1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9b1u RCSB], [https://www.ebi.ac.uk/pdbsum/9b1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9b1u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/B7KXB5_METC4 B7KXB5_METC4]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 2011 discovery of the first rare earth-dependent enzyme in methylotrophic Methylobacterium extorquens AM1 prompted intensive research toward understanding the unique chemistry at play in these systems. This enzyme, an alcohol dehydrogenase (ADH), features a La(3+) ion closely associated with redox-active coenzyme pyrroloquinoline quinone (PQQ) and is structurally homologous to the Ca(2+)-dependent ADH from the same organism. AM1 also produces a periplasmic PQQ-binding protein, PqqT, which we have now structurally characterized to 1.46-A resolution by X-ray diffraction. This crystal structure reveals a Lys residue hydrogen-bonded to PQQ at the site analogously occupied by a Lewis acidic cation in ADH. Accordingly, we prepared K(142)A- and K(142)D-PqqT variants to assess the relevance of this site toward metal binding. Isothermal titration calorimetry experiments and titrations monitored by UV-Vis absorption and emission spectroscopies support that K(142)D-PqqT binds tightly (K(d) = 0.6 +/- 0.2 muM) to La(3+) in the presence of bound PQQ and produces spectral signatures consistent with those of ADH enzymes. These spectral signatures are not observed for WT- or K(142)A-variants or upon addition of Ca(2+) to PQQ ⸦ K(142)D-PqqT. Addition of benzyl alcohol to La(3+)-bound PQQ ⸦ K(142)D-PqqT (but not Ca(2+)-bound PQQ ⸦ K(142)D-PqqT, or La(3+)-bound PQQ ⸦ WT-PqqT) produces spectroscopic changes associated with PQQ reduction, and chemical trapping experiments reveal the production of benzaldehyde, supporting ADH activity. By creating a metal binding site that mimics native ADH enzymes, we present a rare earth-dependent artificial metalloenzyme primed for future mechanistic, biocatalytic, and biosensing applications.
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Authors:
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Structure-driven development of a biomimetic rare earth artificial metalloprotein.,Thompson PJ, Boggs DG, Wilson CA, Bruchs AT, Velidandla U, Bridwell-Rabb J, Olshansky L Proc Natl Acad Sci U S A. 2024 Aug 13;121(33):e2405836121. doi: , 10.1073/pnas.2405836121. Epub 2024 Aug 8. PMID:39116128<ref>PMID:39116128</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9b1u" style="background-color:#fffaf0;"></div>
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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: Methylorubrum extorquens]]
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[[Category: Boggs D]]
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[[Category: Bridwell-Rabb J]]
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[[Category: Bruchs A]]
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[[Category: Olshansky L]]
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[[Category: Thompson P]]

Current revision

Crystal structure of PqqT with PQQ bound

PDB ID 9b1u

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