This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6hrb
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6hrb is ON HOLD Authors: Description: Category: Unreleased Structures) |
|||
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the KdpFABC complex in an E2 inward-facing state (state 2)== | |
| + | <SX load='6hrb' size='340' side='right' viewer='molstar' caption='[[6hrb]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6hrb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HRB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6HRB FirstGlance]. <br> | ||
| + | </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></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hra|6hra]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kdpA, b0698, JW0686 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), kdpB, b0697, JW0685 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), kdpC, b0696, JW0684 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), kdpF, b4513, JW0687 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Potassium-transporting_ATPase Potassium-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.12 3.6.3.12] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6hrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hrb OCA], [http://pdbe.org/6hrb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hrb RCSB], [http://www.ebi.ac.uk/pdbsum/6hrb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hrb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KDPF_ECOLI KDPF_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:23930894). This subunit may be involved in stabilization of the complex (PubMed:10608856).<ref>PMID:10608856</ref> <ref>PMID:23930894</ref> [[http://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> [[http://www.uniprot.org/uniprot/KDPC_ECOLI KDPC_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 acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex (PubMed:21711450).<ref>PMID:21711450</ref> <ref>PMID:23930894</ref> <ref>PMID:2849541</ref> <ref>PMID:8499455</ref> [[http://www.uniprot.org/uniprot/KDPB_ECOLI KDPB_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 is responsible for energy coupling to the transport system (PubMed:16354672).<ref>PMID:16354672</ref> <ref>PMID:23930894</ref> <ref>PMID:2849541</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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6hrb" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Ecoli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Potassium-transporting ATPase]] | ||
| + | [[Category: Azkargorta, M]] | ||
| + | [[Category: Haenelt, I]] | ||
| + | [[Category: Hielkema, L]] | ||
| + | [[Category: Oostergetel, G T]] | ||
| + | [[Category: Paulino, C]] | ||
| + | [[Category: Stock, C]] | ||
| + | [[Category: Tascon, I]] | ||
| + | [[Category: Wunnicke, D]] | ||
| + | [[Category: Membrane protein]] | ||
Current revision
Cryo-EM structure of the KdpFABC complex in an E2 inward-facing state (state 2)
| |||||||||
