View source for 7o17


==ABC transporter NosDFY E154Q, ATP-bound in lipid nanodisc==
<StructureSection load='7o17' size='340' side='right'caption='[[7o17]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7o17]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] and [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri_ATCC_14405_=_CCUG_16156 Pseudomonas stutzeri ATCC 14405 = CCUG 16156]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O17 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5&#8491;</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=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=7o17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o17 OCA], [https://pdbe.org/7o17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o17 RCSB], [https://www.ebi.ac.uk/pdbsum/7o17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o17 ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== Publication Abstract from PubMed ==
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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7o17" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas stutzeri]]
[[Category: Pseudomonas stutzeri ATCC 14405 = CCUG 16156]]
[[Category: Du J]]
[[Category: Einsle O]]
[[Category: Lu W]]
[[Category: Mueller C]]
[[Category: Zhang L]]