Phosphoryl transfer and calcium ion occlusion in the calcium pump

被引：368

作者：

Sorensen, TLM

Moller, JV

Nissen, P

机构：

[1] Aarhus Univ, Dept Biophys, DK-8000 Aarhus C, Denmark

[2] Aarhus Univ, Dept Mol Biol, DK-8000 Aarhus C, Denmark

来源：

SCIENCE | 2004年 / 304卷 / 5677期

关键词：

D O I：

10.1126/science.1099366

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A tight coupling between adenosine triphosphate (ATP) hydrolysis and vectorial ion transport has to be maintained by ATP-consuming ion pumps. We report two crystal structures of Ca2+-bound sarco(endo) plasmic reticulum Ca2+- adenosine triphosphatase (SERCA) at 2.6 and 2.9 angstrom resolution in complex with (i) a nonhydrolyzable ATP analog [adenosine (beta-gamma methylene) triphosphate] and (ii) adenosine diphosphate plus aluminum fluoride. SERCA reacts with ATP by an associative mechanism mediated by two Mg2+ ions to form an aspartyl-phosphorylated intermediate state (Ca-2- E1 similar to P). The conformational changes that accompany the reaction with ATP pull the transmembrane helices 1 and 2 and close a cytosolic entrance for Ca2+, thereby preventing backflow before Ca2+ is released on the other side of the membrane.

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页码：1672 / 1675

页数：4

相关论文

共 25 条

[1] Dissection of the functional domains of the sarcoplasmic reticulum Ca2+-ATPase by site-directed mutagenesis [J].

Andersen, JP .

BIOSCIENCE REPORTS, 1995, 15 (05) :243-261

[2] The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold [J].

Aravind, L ;

Galperin, MY ;

Koonin, EV .

TRENDS IN BIOCHEMICAL SCIENCES, 1998, 23 (04) :127-129

[3] Evolution of substrate specificities in the P-type ATPase superfamily [J].

Axelsen, KB ;

Palmgren, MG .

JOURNAL OF MOLECULAR EVOLUTION, 1998, 46 (01) :84-101

[4] LOCATION OF HIGH-AFFINITY CA-2+-BINDING SITES WITHIN THE PREDICTED TRANSMEMBRANE DOMAIN OF THE SARCOPLASMIC-RETICULUM CA-2+-ATPASE [J].

CLARKE, DM ;

LOO, TW ;

INESI, G ;

MACLENNAN, DH .

NATURE, 1989, 339 (6224) :476-478

[5] Importance of conserved N-domain residues Thr441, Glu442, Lys515, Arg560, and Leu562 of sarcoplasmic reticulum Ca2+-ATPase for MgATP binding and subsequent catalytic steps -: Plasticity of the nucleotide-binding site [J].

Clausen, JD ;

McIntosh, DB ;

Vilsen, B ;

Woolley, DG ;

Andersen, JP .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (22) :20245-20258

[6] CA2+ BINDING TO OCCLUDED SITES IN THE CRATP-ATPASE COMPLEX OF SARCOPLASMIC-RETICULUM - EVIDENCE FOR 2 INDEPENDENT HIGH-AFFINITY SITES [J].

COAN, C ;

JI, JY ;

AMARAL, JA .

BIOCHEMISTRY, 1994, 33 (12) :3722-3731

[7] OCCLUSION OF DIVALENT-CATIONS IN THE PHOSPHORYLATED CALCIUM-PUMP OF SARCOPLASMIC-RETICULUM [J].

DUPONT, Y .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1980, 109 (01) :231-238

[8] ADENOSINE TRIPHOSPHATE-LINKED CONCENTRATION OF CALCIUM IONS IN A PARTICULATE FRACTION OF RABBIT MUSCLE [J].

EBASHI, S ;

LIPMANN, F .

JOURNAL OF CELL BIOLOGY, 1962, 14 (03) :389-&

[9] Importance of transmembrane segment M1 of the sarcoplasmic reticulum Ca2+-ATPase in Ca2+ occlusion and phosphoenzyme processing [J].

Einholm, AP ;

Vilsen, B ;

Andersen, JP .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (16) :15888-15896

[10]

HASSELBACH W, 1961, BIOCHEM Z, V333, P518