7nnp

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Rb-loaded cryo-EM structure of the E1-ATP KdpFABC complex.

Structural highlights

7nnp is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.2Å
Ligands:ACP, CDL, RB
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

KdpFABC, a high-affinity K(+) pump, combines the ion channel KdpA and the P-type ATPase KdpB to secure survival at K(+) limitation. Here, we apply a combination of cryo-EM, biochemical assays, and MD simulations to illuminate the mechanisms underlying transport and the coupling to ATP hydrolysis. We show that ions are transported via an intersubunit tunnel through KdpA and KdpB. At the subunit interface, the tunnel is constricted by a phenylalanine, which, by polarized cation-pi stacking, controls K(+) entry into the canonical substrate binding site (CBS) of KdpB. Within the CBS, ATPase coupling is mediated by the charge distribution between an aspartate and a lysine. Interestingly, individual elements of the ion translocation mechanism of KdpFABC identified here are conserved among a wide variety of P-type ATPases from different families. This leads us to the hypothesis that KdpB might represent an early descendant of a common ancestor of cation pumps.

Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC.,Silberberg JM, Corey RA, Hielkema L, Stock C, Stansfeld PJ, Paulino C, Hanelt I Nat Commun. 2021 Aug 24;12(1):5098. doi: 10.1038/s41467-021-25242-x. PMID:34429416[5]

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

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Citations
1 reviews cite this structure
P-type ATPases: Many more enigmas left to solve.
Palmgren et al. (2023)
0 more
3 other articles
No citations found

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ Silberberg JM, Corey RA, Hielkema L, Stock C, Stansfeld PJ, Paulino C, Hänelt I. Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC. Nat Commun. 2021 Aug 24;12(1):5098. PMID:34429416 doi:10.1038/s41467-021-25242-x

Contents


PDB ID 7nnp

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