Structural and biochemical analysis of the Obg GTP binding protein

被引：150

作者：

Buglino, J ^{[1
]}

Shen, V ^{[1
]}

Hakimian, P ^{[1
]}

Lima, CD ^{[1
]}

机构：

[1] Cornell Univ, Weill Med Coll, Dept Biochem, Struct Biol Program, New York, NY 10021 USA

来源：

STRUCTURE | 2002年 / 10卷 / 11期

关键词：

D O I：

10.1016/S0969-2126(02)00882-1

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 Obg nucleotide binding protein family has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to man. Members of the family contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain. Structural analysis of Bacillus subtilis Obg revealed respective domain architectures and how they are coupled through the putative switch elements of the C-terminal GTPase domain in apo and nucleotide-bound configurations. Biochemical analysis of bacterial and human Obg proteins combined with the structural observation of the ppGpp nucleotide within the Obg active sight suggest a potential role for ppGpp modulation of Obg function in B. subtilis.

引用

页码：1581 / 1592

页数：12

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