3-DIMENSIONAL STRUCTURE OF NA, K-ATPASE DETERMINED FROM MEMBRANE CRYSTALS INDUCED BY COBALT TETRAMINE ATP

被引：22
作者：
SKRIVER, E
KAVEUS, U
HEBERT, H
MAUNSBACH, AB
机构：
[1] AARHUS UNIV,DANISH BIOMEMBRANE RES CTR,DK-8000 AARHUS,DENMARK
[2] KAROLINSKA INST,CTR STRUCT BIOCHEM,S-14157 HUDDINGE,SWEDEN
来源：
JOURNAL OF STRUCTURAL BIOLOGY | 1992年 / 108卷 / 02期
关键词：
D O I：
10.1016/1047-8477(92)90017-5
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The three-dimensional structure of Na,K-ATPase has been analyzed with electron microscopy and image processing. The enzyme, purified from pig kidney outer medulla, was arranged in a new form of tetragonal two-dimensional membrane crystals after incubation with cobalt-tetrammine-ATP, a stable MgATP complex analogue. Each continuous protein domain, as delineated by negative stain, consists of two αβ-protomers related by a dyad axis. The two rod-like regions are connected by a bridge displaced about 20 Å away from the center of the structure toward the lipid bilayer. The domain connecting the two protomers is more constricted and closer to the center of the stucture in the Co(NH3)4ATP-induced crystals than in the vanadate-induced p21 crystals. These observations suggest that the difference between previously analyzed dimers of two-dimensional p21 crystals induced with vanadate/magnesium and dimers of p4 crystals induced with Co(NH3)4ATP reflects two different conformational states of the enzyme. © 1992.
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页码：176 / 185
页数：10
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