7z17: Difference between revisions
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==E. coli C-P lyase bound to a PhnK ABC dimer in an open conformation== | |||
<StructureSection load='7z17' size='340' side='right'caption='[[7z17]], [[Resolution|resolution]] 2.57Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7z17]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z17 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]] 2.57Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=I9X:alpha-D-ribose-1,2-cyclic-phosphate-5-phosphate'>I9X</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7z17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z17 OCA], [https://pdbe.org/7z17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z17 RCSB], [https://www.ebi.ac.uk/pdbsum/7z17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z17 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PHNK_ECOLI PHNK_ECOLI] Belongs to an operon involved in alkylphosphonate uptake and C-P lyase. Exact function not known. PhnK is not required for the ribophosphonate triphosphate (RPnTP) synthase reaction. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Escherichia coli, the 14-cistron phn operon encoding carbon-phosphorus lyase allows for utilisation of phosphorus from a wide range of stable phosphonate compounds containing a C-P bond. As part of a complex, multi-step pathway, the PhnJ subunit was shown to cleave the C-P bond via a radical mechanism, however, the details of the reaction could not immediately be reconciled with the crystal structure of a 220 kDa PhnGHIJ C-P lyase core complex, leaving a significant gap in our understanding of phosphonate breakdown in bacteria. Here, we show using single-particle cryogenic electron microscopy that PhnJ mediates binding of a double dimer of the ATP-binding cassette proteins, PhnK and PhnL, to the core complex. ATP hydrolysis induces drastic structural remodelling leading to opening of the core complex and reconfiguration of a metal-binding and putative active site located at the interface between the PhnI and PhnJ subunits. | |||
Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.,Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE Nat Commun. 2023 Feb 22;14(1):1001. doi: 10.1038/s41467-023-36604-y. PMID:36813778<ref>PMID:36813778</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7z17" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Amstrup SK]] | |||
[[Category: Boesen T]] | |||
[[Category: Brodersen DE]] | |||
[[Category: Enghild JJ]] | |||
[[Category: Hove-Jensen B]] | |||
[[Category: Karlsen JL]] | |||
[[Category: Skjerning RB]] | |||
[[Category: Sofos N]] | |||
