Publication

Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels

Stock, C., Hielkema, L., Tascón, I., Wunnicke, D., Oostergetel, G. T., Azkargorta, M., Paulino, C. & Hänelt, I., 26-Nov-2018, In : Nature Communications. 9, 1, 10 p., 4971.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Stock, C., Hielkema, L., Tascón, I., Wunnicke, D., Oostergetel, G. T., Azkargorta, M., ... Hänelt, I. (2018). Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels. Nature Communications, 9(1), [4971]. https://doi.org/10.1038/s41467-018-07319-2

Author

Stock, C ; Hielkema, L ; Tascón, I ; Wunnicke, D ; Oostergetel, G T ; Azkargorta, M ; Paulino, C ; Hänelt, I. / Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels. In: Nature Communications. 2018 ; Vol. 9, No. 1.

Harvard

Stock, C, Hielkema, L, Tascón, I, Wunnicke, D, Oostergetel, GT, Azkargorta, M, Paulino, C & Hänelt, I 2018, 'Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels' Nature Communications, vol. 9, no. 1, 4971. https://doi.org/10.1038/s41467-018-07319-2

Standard

Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels. / Stock, C; Hielkema, L; Tascón, I; Wunnicke, D; Oostergetel, G T; Azkargorta, M; Paulino, C; Hänelt, I.

In: Nature Communications, Vol. 9, No. 1, 4971, 26.11.2018.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Stock C, Hielkema L, Tascón I, Wunnicke D, Oostergetel GT, Azkargorta M et al. Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels. Nature Communications. 2018 Nov 26;9(1). 4971. https://doi.org/10.1038/s41467-018-07319-2


BibTeX

@article{05811c18a2634fa28e71ee0d1fe538b2,
title = "Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels",
abstract = "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 {\AA} and 4.0 {\AA} 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.",
keywords = "P-TYPE ATPASE, AMINO-ACID SUBSTITUTIONS, MEMBRANE REGION M-2C2, UPTAKE SYSTEM KTRAB, ESCHERICHIA-COLI, KDP-ATPASE, PHOSPHORYLATION SITE, CATION-TRANSPORT, ASPARTIC-ACID, HIGH-AFFINITY",
author = "C Stock and L Hielkema and I Tasc{\'o}n and D Wunnicke and Oostergetel, {G T} and M Azkargorta and C Paulino and I H{\"a}nelt",
year = "2018",
month = "11",
day = "26",
doi = "10.1038/s41467-018-07319-2",
language = "English",
volume = "9",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels

AU - Stock, C

AU - Hielkema, L

AU - Tascón, I

AU - Wunnicke, D

AU - Oostergetel, G T

AU - Azkargorta, M

AU - Paulino, C

AU - Hänelt, I

PY - 2018/11/26

Y1 - 2018/11/26

N2 - 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 Å and 4.0 Å 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.

AB - 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 Å and 4.0 Å 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.

KW - P-TYPE ATPASE

KW - AMINO-ACID SUBSTITUTIONS

KW - MEMBRANE REGION M-2C2

KW - UPTAKE SYSTEM KTRAB

KW - ESCHERICHIA-COLI

KW - KDP-ATPASE

KW - PHOSPHORYLATION SITE

KW - CATION-TRANSPORT

KW - ASPARTIC-ACID

KW - HIGH-AFFINITY

U2 - 10.1038/s41467-018-07319-2

DO - 10.1038/s41467-018-07319-2

M3 - Article

VL - 9

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 4971

ER -

ID: 71527343