6hra: Difference between revisions

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-'''Unreleased structure'''
-The entry 6hra is ON HOLD  until Paper Publication
+==Cryo-EM structure of the KdpFABC complex in an E1 outward-facing state (state 1)==
+<SX load='6hra' size='340' side='right' viewer='molstar' caption='[[6hra]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6hra]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HRA 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]] 3.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=6hra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hra OCA], [https://pdbe.org/6hra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hra RCSB], [https://www.ebi.ac.uk/pdbsum/6hra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hra 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 ==
+P-type ATPases ubiquitously pump cations across biological membranes to maintain vital ion gradients. Among those, the chimeric K(+) uptake system KdpFABC is unique. While ATP hydrolysis is accomplished by the P-type ATPase subunit KdpB, K(+) has been assumed to be transported by the channel-like subunit KdpA. A first crystal structure uncovered its overall topology, suggesting such a spatial separation of energizing and transporting units. Here, we report two cryo-EM structures of the 157 kDa, asymmetric KdpFABC complex at 3.7 A and 4.0 A resolution in an E1 and an E2 state, respectively. Unexpectedly, the structures suggest a translocation pathway through two half-channels along KdpA and KdpB, uniting the alternating-access mechanism of actively pumping P-type ATPases with the high affinity and selectivity of K(+) channels. This way, KdpFABC would function as a true chimeric complex, synergizing the best features of otherwise separately evolved transport mechanisms.
-Authors:
+Cryo-EM structures of KdpFABC suggest a K(+) transport mechanism via two inter-subunit half-channels.,Stock C, Hielkema L, Tascon I, Wunnicke D, Oostergetel GT, Azkargorta M, Paulino C, Hanelt I Nat Commun. 2018 Nov 26;9(1):4971. doi: 10.1038/s41467-018-07319-2. PMID:30478378<ref>PMID:30478378</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6hra" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Azkargorta M]]
+[[Category: Haenelt I]]
+[[Category: Hielkema L]]
+[[Category: Oostergetel GT]]
+[[Category: Paulino C]]
+[[Category: Stock C]]
+[[Category: Tascon I]]
+[[Category: Wunnicke D]]