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1lnz

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{{STRUCTURE_1lnz| PDB=1lnz | SCENE= }}
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'''Structure of the Obg GTP-binding protein'''
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===Structure of the Obg GTP-binding protein===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12429099}}
==About this Structure==
==About this Structure==
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[[Category: Stringent factor]]
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Revision as of 18:32, 2 July 2008

Image:1lnz.png

Template:STRUCTURE 1lnz

Structure of the Obg GTP-binding protein

Template:ABSTRACT PUBMED 12429099

About this Structure

1LNZ is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structural and biochemical analysis of the Obg GTP binding protein., Buglino J, Shen V, Hakimian P, Lima CD, Structure. 2002 Nov;10(11):1581-92. PMID:12429099

Page seeded by OCA on Wed Jul 2 21:32:00 2008

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