A large conformational change of the translocation ATPase SecA

被引：124
作者：
Osborne, AR [1 ]
Clemons, WM [1 ]
Rapoport, TA [1 ]
机构：
[1] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2004年 / 101卷 / 30期
关键词：
D O I：
10.1073/pnas.0401742101
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：
The ATPase SecA mediates the posttranslational translocation of a wide range of polypeptide substrates through the SecY channel in the cytoplasmic membrane of bacteria. We have determined the crystal structure of a monomeric form of Bacillus subtilis SecA at a 2.2-Angstrom resolution. A comparison with the previously determined structures of SecA reveals a nucleotide-independent, large conformational change that opens a deep groove similar to that in other proteins that interact with diverse polypeptides. We propose that the open form of SecA represents an activated state.
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收藏
页码：10937 / 10942
页数：6
相关论文
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