Rearrangement of boundary, stand-by, and fluid lipids during the formation of two-dimensional crystals of Ca2+-ATPase

G. Szakonyi, L. Dux, L. I. Horváth

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Ca2+-transport ATPase of sarcoplasmic reticulum of rabbit skeletal and carp abdominal muscle is essential for the removal of large amounts of Ca2+ ions during the relaxation of the muscle. As in the case of other lipid- protein systems, fluid lipid and motionally restricted boundary lipid sites lead to multicomponent spin label EPR spectra. Having subtracted the dominating fluid component a two-component lineshape is recovered as a subtraction endpoint, suggesting the presence of a third, motionally less restricted stand-by lipid shell as fraction of boundary lipids. On adding 5 mM decavanadate the phosphate binding site is blocked and the protein dimers form a two dimensional array, at least in the case of the sarcoplasmic reticulum of rabbit. During two-dimensional crystal formation of rabbit Ca2+-ATPase an increase of lipids was found in boundary and standby shells. No such change was observed in the case of the sarcoplasmic reticulum of carp abdominal muscle.

Original languageEnglish
Pages (from-to)253-256
Number of pages4
JournalJournal of Molecular Structure
Volume482-483
DOIs
Publication statusPublished - May 25 1999

Fingerprint

Calcium-Transporting ATPases
lipids
sarcoplasmic reticulum
Lipids
Crystals
Fluids
fluids
rabbits
Sarcoplasmic Reticulum
muscles
crystals
Muscle
Abdominal Muscles
Carps
Rabbits
proteins
Spin Labels
Muscle Relaxation
Vanadates
subtraction

Keywords

  • Lipid analogue label
  • Lipid exclusion
  • Lipid locking
  • Spin label EPR
  • Two- dimensional crystals of Ca-ATPase

ASJC Scopus subject areas

  • Structural Biology
  • Organic Chemistry
  • Physical and Theoretical Chemistry
  • Spectroscopy
  • Atomic and Molecular Physics, and Optics

Cite this

Rearrangement of boundary, stand-by, and fluid lipids during the formation of two-dimensional crystals of Ca2+-ATPase. / Szakonyi, G.; Dux, L.; Horváth, L. I.

In: Journal of Molecular Structure, Vol. 482-483, 25.05.1999, p. 253-256.

Research output: Contribution to journalArticle

@article{f74e7d46bd834c5b94eb0c0c0f6e7cbf,
title = "Rearrangement of boundary, stand-by, and fluid lipids during the formation of two-dimensional crystals of Ca2+-ATPase",
abstract = "Ca2+-transport ATPase of sarcoplasmic reticulum of rabbit skeletal and carp abdominal muscle is essential for the removal of large amounts of Ca2+ ions during the relaxation of the muscle. As in the case of other lipid- protein systems, fluid lipid and motionally restricted boundary lipid sites lead to multicomponent spin label EPR spectra. Having subtracted the dominating fluid component a two-component lineshape is recovered as a subtraction endpoint, suggesting the presence of a third, motionally less restricted stand-by lipid shell as fraction of boundary lipids. On adding 5 mM decavanadate the phosphate binding site is blocked and the protein dimers form a two dimensional array, at least in the case of the sarcoplasmic reticulum of rabbit. During two-dimensional crystal formation of rabbit Ca2+-ATPase an increase of lipids was found in boundary and standby shells. No such change was observed in the case of the sarcoplasmic reticulum of carp abdominal muscle.",
keywords = "Lipid analogue label, Lipid exclusion, Lipid locking, Spin label EPR, Two- dimensional crystals of Ca-ATPase",
author = "G. Szakonyi and L. Dux and Horv{\'a}th, {L. I.}",
year = "1999",
month = "5",
day = "25",
doi = "10.1016/S0022-2860(98)00666-8",
language = "English",
volume = "482-483",
pages = "253--256",
journal = "Journal of Molecular Structure",
issn = "0022-2860",
publisher = "Elsevier",

}

TY - JOUR

T1 - Rearrangement of boundary, stand-by, and fluid lipids during the formation of two-dimensional crystals of Ca2+-ATPase

AU - Szakonyi, G.

AU - Dux, L.

AU - Horváth, L. I.

PY - 1999/5/25

Y1 - 1999/5/25

N2 - Ca2+-transport ATPase of sarcoplasmic reticulum of rabbit skeletal and carp abdominal muscle is essential for the removal of large amounts of Ca2+ ions during the relaxation of the muscle. As in the case of other lipid- protein systems, fluid lipid and motionally restricted boundary lipid sites lead to multicomponent spin label EPR spectra. Having subtracted the dominating fluid component a two-component lineshape is recovered as a subtraction endpoint, suggesting the presence of a third, motionally less restricted stand-by lipid shell as fraction of boundary lipids. On adding 5 mM decavanadate the phosphate binding site is blocked and the protein dimers form a two dimensional array, at least in the case of the sarcoplasmic reticulum of rabbit. During two-dimensional crystal formation of rabbit Ca2+-ATPase an increase of lipids was found in boundary and standby shells. No such change was observed in the case of the sarcoplasmic reticulum of carp abdominal muscle.

AB - Ca2+-transport ATPase of sarcoplasmic reticulum of rabbit skeletal and carp abdominal muscle is essential for the removal of large amounts of Ca2+ ions during the relaxation of the muscle. As in the case of other lipid- protein systems, fluid lipid and motionally restricted boundary lipid sites lead to multicomponent spin label EPR spectra. Having subtracted the dominating fluid component a two-component lineshape is recovered as a subtraction endpoint, suggesting the presence of a third, motionally less restricted stand-by lipid shell as fraction of boundary lipids. On adding 5 mM decavanadate the phosphate binding site is blocked and the protein dimers form a two dimensional array, at least in the case of the sarcoplasmic reticulum of rabbit. During two-dimensional crystal formation of rabbit Ca2+-ATPase an increase of lipids was found in boundary and standby shells. No such change was observed in the case of the sarcoplasmic reticulum of carp abdominal muscle.

KW - Lipid analogue label

KW - Lipid exclusion

KW - Lipid locking

KW - Spin label EPR

KW - Two- dimensional crystals of Ca-ATPase

UR - http://www.scopus.com/inward/record.url?scp=0033602963&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033602963&partnerID=8YFLogxK

U2 - 10.1016/S0022-2860(98)00666-8

DO - 10.1016/S0022-2860(98)00666-8

M3 - Article

AN - SCOPUS:0033602963

VL - 482-483

SP - 253

EP - 256

JO - Journal of Molecular Structure

JF - Journal of Molecular Structure

SN - 0022-2860

ER -