9c4o

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m (Protected "9c4o" [edit=sysop:move=sysop])
Current revision (05:58, 19 June 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9c4o is ON HOLD
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==Cryo-EM structure of PqqU with ligand PQQ==
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<StructureSection load='9c4o' size='340' side='right'caption='[[9c4o]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
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Authors: Munder, F., Venugopal, H., Grinter, R.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9c4o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BW25113 Escherichia coli BW25113]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9C4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C4O FirstGlance]. <br>
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Description: Cryo-EM structure of PqqU with ligand PQQ
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 1.99&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene></td></tr>
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[[Category: Munder, F]]
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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=9c4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c4o OCA], [https://pdbe.org/9c4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c4o RCSB], [https://www.ebi.ac.uk/pdbsum/9c4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c4o ProSAT]</span></td></tr>
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[[Category: Grinter, R]]
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</table>
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[[Category: Venugopal, H]]
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== Function ==
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[https://www.uniprot.org/uniprot/PQQU_ECOLI PQQU_ECOLI] Mediates the TonB-dependent high affinity transport across the outer membrane of pyrroloquinoline quinone (PQQ), a redox cofactor required for the activity of Gcd and Asd dehydrogenases (PubMed:36054785). The uptake process is energised via the TonB-ExbBD complex (PubMed:36054785). Not involved in the transport of an iron-containing substrate under laboratory conditions (PubMed:32355044, PubMed:36054785).<ref>PMID:32355044</ref> <ref>PMID:36054785</ref>
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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: Escherichia coli BW25113]]
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[[Category: Large Structures]]
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[[Category: Grinter R]]
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[[Category: Munder F]]
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[[Category: Venugopal H]]

Current revision

Cryo-EM structure of PqqU with ligand PQQ

PDB ID 9c4o

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