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The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation

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The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation. / Hansen, Sara Basse; Dyla, Mateusz; Neumann, Caroline et al.

In: Journal of Molecular Biology, Vol. 433, No. 16, 167015, 08.2021.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Hansen SB, Dyla M, Neumann C, Quistgaard EMH, Andersen JL, Kjaergaard M et al. The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation. Journal of Molecular Biology. 2021 Aug;433(16):167015. doi: 10.1016/j.jmb.2021.167015

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@article{0f72028227dd4d8f8b0c3ac08bac9f0b,
title = "The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation",
abstract = "Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). Here we present three crystal structures of Ca2+-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF3- mimicking a phosphoenzyme state reveal a closed state, which is intermediate between the outward-open E2P and the proton-occluded E2-P* conformations known for SERCA. It suggests that LMCA1 in the E2P state is pre-organized for dephosphorylation upon Ca2+ release, consistent with the rapid dephosphorylation observed in single-molecule studies. An arginine side-chain occupies the position equivalent to calcium binding site I in SERCA, leaving a single Ca2+ binding site in LMCA1, corresponding to SERCA site II. Observing no putative transport pathways dedicated to protons, we infer a direct proton counter transport through the Ca2+ exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters.",
keywords = "Ca-ATPase LMCA1, calcium, Listeria, membrane protein crystallography, P-type ATPase",
author = "Hansen, {Sara Basse} and Mateusz Dyla and Caroline Neumann and Quistgaard, {Esben Meldgaard Hoegh} and Andersen, {Jacob Lauwring} and Magnus Kjaergaard and Poul Nissen",
note = "Publisher Copyright: {\textcopyright} 2021 The Authors",
year = "2021",
month = aug,
doi = "10.1016/j.jmb.2021.167015",
language = "English",
volume = "433",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "16",

}

RIS

TY - JOUR

T1 - The Crystal Structure of the Ca2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation

AU - Hansen, Sara Basse

AU - Dyla, Mateusz

AU - Neumann, Caroline

AU - Quistgaard, Esben Meldgaard Hoegh

AU - Andersen, Jacob Lauwring

AU - Kjaergaard, Magnus

AU - Nissen, Poul

N1 - Publisher Copyright: © 2021 The Authors

PY - 2021/8

Y1 - 2021/8

N2 - Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). Here we present three crystal structures of Ca2+-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF3- mimicking a phosphoenzyme state reveal a closed state, which is intermediate between the outward-open E2P and the proton-occluded E2-P* conformations known for SERCA. It suggests that LMCA1 in the E2P state is pre-organized for dephosphorylation upon Ca2+ release, consistent with the rapid dephosphorylation observed in single-molecule studies. An arginine side-chain occupies the position equivalent to calcium binding site I in SERCA, leaving a single Ca2+ binding site in LMCA1, corresponding to SERCA site II. Observing no putative transport pathways dedicated to protons, we infer a direct proton counter transport through the Ca2+ exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters.

AB - Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). Here we present three crystal structures of Ca2+-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF3- mimicking a phosphoenzyme state reveal a closed state, which is intermediate between the outward-open E2P and the proton-occluded E2-P* conformations known for SERCA. It suggests that LMCA1 in the E2P state is pre-organized for dephosphorylation upon Ca2+ release, consistent with the rapid dephosphorylation observed in single-molecule studies. An arginine side-chain occupies the position equivalent to calcium binding site I in SERCA, leaving a single Ca2+ binding site in LMCA1, corresponding to SERCA site II. Observing no putative transport pathways dedicated to protons, we infer a direct proton counter transport through the Ca2+ exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters.

KW - Ca-ATPase LMCA1

KW - calcium

KW - Listeria

KW - membrane protein crystallography

KW - P-type ATPase

UR - http://www.scopus.com/inward/record.url?scp=85106389288&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2021.167015

DO - 10.1016/j.jmb.2021.167015

M3 - Journal article

C2 - 33933469

AN - SCOPUS:85106389288

VL - 433

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 16

M1 - 167015

ER -