A common topology of proteins catalyzing ATP‐triggered reactions

FEBS Letters

Amano, Toyoki¹  Yoshida, Masasuke¹ 

[1] Research Laboratory of Resources Utilization, R-1, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 227, Japan

关键词: ATP binding domain;    ABC transporter;    MDR folding;    SecA folding;    Lon protease;    Proteasome;    MF1;    F1-ATPase from a bovine heart mitochondria;   

DOI  :  10.1016/0014-5793(94)01438-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A protein fold, six parallel β strands surrounding the central α helix, is likely to be a common structure in protein families known to have a typical set of nucleotide binding consensus sequenced motifs A and B and to catalyze ATP-triggered reactions. According to this ATP-triggered protein fold, the conserved Glu (or Asp), which acts as a general base to activate a water molecule for an in-line attack of the γ-phosphate, is at the exit of the second β strand. The fifth β strand may be involved in propagation of conformational change triggered by ATP hydrolysis.

【 授权许可】

Unknown