7qba
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7qba]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBA FirstGlance]. <br> | <table><tr><td colspan='2'>[[7qba]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBA FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.78Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=7qba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qba OCA], [https://pdbe.org/7qba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qba RCSB], [https://www.ebi.ac.uk/pdbsum/7qba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qba 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=7qba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qba OCA], [https://pdbe.org/7qba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qba RCSB], [https://www.ebi.ac.uk/pdbsum/7qba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qba ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/NOSD_STUST NOSD_STUST] Required for the assembly of the copper chromophores of nitrous oxide reductase (PubMed:2170125). Could be part of the ABC transporter complex NosDFY (Probable).<ref>PMID:2170125</ref> <ref>PMID:12618453</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | Emissions of the critical ozone-depleting and greenhouse gas nitrous oxide ( | + | Emissions of the critical ozone-depleting and greenhouse gas nitrous oxide (N(2)O) from soils and industrial processes have increased considerably over the last decades(1-3). As the final step of bacterial denitrification, N(2)O is reduced to chemically inert N(2) (refs. (1,4)) in a reaction that is catalysed by the copper-dependent nitrous oxide reductase (N(2)OR) (ref. (5)). The assembly of its unique [4Cu:2S] active site cluster Cu(Z) requires both the ATP-binding-cassette (ABC) complex NosDFY and the membrane-anchored copper chaperone NosL (refs. (4,6)). Here we report cryo-electron microscopy structures of Pseudomonas stutzeri NosDFY and its complexes with NosL and N(2)OR, respectively. We find that the periplasmic NosD protein contains a binding site for a Cu(+) ion and interacts specifically with NosL in its nucleotide-free state, whereas its binding to N(2)OR requires a conformational change that is triggered by ATP binding. Mutually exclusive structures of NosDFY in complex with NosL and with N(2)OR reveal a sequential metal-trafficking and assembly pathway for a highly complex copper site. Within this pathway, NosDFY acts as a mechanical energy transducer rather than as a transporter. It links ATP hydrolysis in the cytoplasm to a conformational transition of the NosD subunit in the periplasm, which is required for NosDFY to switch its interaction partner so that copper ions are handed over from the chaperone NosL to the enzyme N(2)OR. |
| - | Molecular interplay of an assembly machinery for nitrous oxide reductase.,Muller C, Zhang L, Zipfel S, Topitsch A, Lutz M, Eckert J, Prasser B, Chami M, Lu W, Du J, Einsle O Nature. 2022 Aug;608(7923):626-631. doi: 10.1038/s41586-022-05015-2. Epub 2022, Jul 27. PMID:35896743<ref>PMID:35896743</ref> | + | Molecular interplay of an assembly machinery for nitrous oxide reductase.,Muller C, Zhang L, Zipfel S, Topitsch A, Lutz M, Eckert J, Prasser B, Chami M, Lu W, Du J, Einsle O Nature. 2022 Aug;608(7923):626-631. doi: 10.1038/s41586-022-05015-2. Epub 2022 , Jul 27. PMID:35896743<ref>PMID:35896743</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
CryoEM structure of the ABC transporter NosDFY complexed with nitrous oxide reductase NosZ
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