6hra

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM structure of the KdpFABC complex in an E1 outward-facing state (state 1)

6hra, resolution 3.70Å

Structural highlights

6hra is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.7Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Damnjanovic B, Weber A, Potschies M, Greie JC, Apell HJ. Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase. Biochemistry. 2013 Aug 20;52(33):5563-76. doi: 10.1021/bi400729e. Epub 2013 Aug, 9. PMID:23930894 doi:http://dx.doi.org/10.1021/bi400729e
↑ Siebers A, Altendorf K. The K+-translocating Kdp-ATPase from Escherichia coli. Purification, enzymatic properties and production of complex- and subunit-specific antisera. Eur J Biochem. 1988 Dec 1;178(1):131-40. PMID:2849541
↑ Buurman ET, Kim KT, Epstein W. Genetic evidence for two sequentially occupied K+ binding sites in the Kdp transport ATPase. J Biol Chem. 1995 Mar 24;270(12):6678-85. PMID:7896809
↑ Kollmann R, Altendorf K. ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli. Biochim Biophys Acta. 1993 Jun 10;1143(1):62-6. PMID:8499455
↑ Stock C, Hielkema L, Tascon I, Wunnicke D, Oostergetel GT, Azkargorta M, Paulino C, Hanelt I. Cryo-EM structures of KdpFABC suggest a K(+) transport mechanism via two inter-subunit half-channels. Nat Commun. 2018 Nov 26;9(1):4971. doi: 10.1038/s41467-018-07319-2. PMID:30478378 doi:http://dx.doi.org/10.1038/s41467-018-07319-2

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6hra"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6hra is ON HOLD
+==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]]

6hra

From Proteopedia

Current revision

Cryo-EM structure of the KdpFABC complex in an E1 outward-facing state (state 1)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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