7zrk: Difference between revisions
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==Cryo-EM map of the WT KdpFABC complex in the E1-P_ADP conformation, under turnover conditions== | |||
<StructureSection load='7zrk' size='340' side='right'caption='[[7zrk]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7zrk]] is a 4 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=7ZRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZRK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=7zrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zrk OCA], [https://pdbe.org/7zrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zrk RCSB], [https://www.ebi.ac.uk/pdbsum/7zrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zrk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KDPA_ECOLI KDPA_ECOLI] Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:2849541, PubMed:8499455, PubMed:23930894). This subunit binds and transports the potassium across the cytoplasmic membrane (PubMed:7896809).<ref>PMID:23930894</ref> <ref>PMID:2849541</ref> <ref>PMID:7896809</ref> <ref>PMID:8499455</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
KdpFABC is a high-affinity prokaryotic K<sup>+</sup> uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K<sup>+</sup> levels, KdpFABC needs to be inhibited to prevent excessive K<sup>+</sup> accumulation to the point of toxicity. This is achieved by a phosphorylation of the serine residue in the TGES<sub>162</sub> motif in the A domain of the pump subunit KdpB (KdpB<sub>S162-P</sub>). Here, we explore the structural basis of inhibition by KdpB<sub>S162</sub> phosphorylation by determining the conformational landscape of KdpFABC under inhibiting and non-inhibiting conditions. Under turnover conditions, we identified a new inhibited KdpFABC state that we termed E1P tight, which is not part of the canonical Post-Albers transport cycle of P-type ATPases. It likely represents the biochemically described stalled E1P state adopted by KdpFABC upon KdpB<sub>S162</sub> phosphorylation. The E1P tight state exhibits a compact fold of the three cytoplasmic domains and is likely adopted when the transition from high-energy E1P states to E2P states is unsuccessful. This study represents a structural characterization of a biologically relevant off-cycle state in the P-type ATPase family and supports the emerging discussion of P-type ATPase regulation by such states. | |||
Inhibited KdpFABC transitions into an E1 off-cycle state.,Silberberg JM, Stock C, Hielkema L, Corey RA, Rheinberger J, Wunnicke D, Dubach VRA, Stansfeld PJ, Hanelt I, Paulino C Elife. 2022 Oct 18;11. pii: 80988. doi: 10.7554/eLife.80988. PMID:36255052<ref>PMID:36255052</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7zrk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Corey RA]] | |||
[[Category: Dubach VRA]] | |||
[[Category: Haenelt I]] | |||
[[Category: Hielkema L]] | |||
[[Category: Paulino C]] | |||
[[Category: Silberberg JM]] | |||
[[Category: Stansfeld PJ]] | |||
[[Category: Stock C]] | |||
[[Category: Wunnicke D]] | |||
Latest revision as of 23:11, 16 November 2022
Cryo-EM map of the WT KdpFABC complex in the E1-P_ADP conformation, under turnover conditionsCryo-EM map of the WT KdpFABC complex in the E1-P_ADP conformation, under turnover conditions
Structural highlights
FunctionKDPA_ECOLI Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:2849541, PubMed:8499455, PubMed:23930894). This subunit binds and transports the potassium across the cytoplasmic membrane (PubMed:7896809).[1] [2] [3] [4] Publication Abstract from PubMedKdpFABC is a high-affinity prokaryotic K<sup>+</sup> uptake system that forms a functional chimera between a channel-like subunit (KdpA) and a P-type ATPase (KdpB). At high K<sup>+</sup> levels, KdpFABC needs to be inhibited to prevent excessive K<sup>+</sup> accumulation to the point of toxicity. This is achieved by a phosphorylation of the serine residue in the TGES<sub>162</sub> motif in the A domain of the pump subunit KdpB (KdpB<sub>S162-P</sub>). Here, we explore the structural basis of inhibition by KdpB<sub>S162</sub> phosphorylation by determining the conformational landscape of KdpFABC under inhibiting and non-inhibiting conditions. Under turnover conditions, we identified a new inhibited KdpFABC state that we termed E1P tight, which is not part of the canonical Post-Albers transport cycle of P-type ATPases. It likely represents the biochemically described stalled E1P state adopted by KdpFABC upon KdpB<sub>S162</sub> phosphorylation. The E1P tight state exhibits a compact fold of the three cytoplasmic domains and is likely adopted when the transition from high-energy E1P states to E2P states is unsuccessful. This study represents a structural characterization of a biologically relevant off-cycle state in the P-type ATPase family and supports the emerging discussion of P-type ATPase regulation by such states. Inhibited KdpFABC transitions into an E1 off-cycle state.,Silberberg JM, Stock C, Hielkema L, Corey RA, Rheinberger J, Wunnicke D, Dubach VRA, Stansfeld PJ, Hanelt I, Paulino C Elife. 2022 Oct 18;11. pii: 80988. doi: 10.7554/eLife.80988. PMID:36255052[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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