1lnz: Difference between revisions

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[[Image:1lnz.~~gif~~|left|200px]]

[[Image:1lnz.png|left|200px]]

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~~'''~~Structure of the Obg GTP-binding protein~~'''~~

===Structure of the Obg GTP-binding protein===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_12429099}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12429099 is the PubMed ID number.

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==About this Structure==

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[[Category: Stringent factor]]

[[Category: Structural genomic]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:06:05 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:32:00 2008''

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-[[Image:1lnz.gif|left|200px]]
+{{Seed}}
+[[Image:1lnz.png|left|200px]]
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 {{STRUCTURE_1lnz|  PDB=1lnz  |  SCENE=  }}
-'''Structure of the Obg GTP-binding protein'''
+===Structure of the Obg GTP-binding protein===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12429099}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12429099 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12429099}}
 ==About this Structure==
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 [[Category: Stringent factor]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:06:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 21:32:00 2008''