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1lnz

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(New page: 200px<br /><applet load="1lnz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lnz, resolution 2.60&Aring;" /> '''Structure of the Obg...)
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[[Image:1lnz.gif|left|200px]]<br /><applet load="1lnz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lnz.gif|left|200px]]<br /><applet load="1lnz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lnz, resolution 2.60&Aring;" />
caption="1lnz, resolution 2.60&Aring;" />
'''Structure of the Obg GTP-binding protein'''<br />
'''Structure of the Obg GTP-binding protein'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1LNZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and G4P as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LNZ OCA].
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1LNZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=G4P:'>G4P</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNZ OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Buglino, J.]]
[[Category: Buglino, J.]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
[[Category: Hakimian, P.]]
[[Category: Hakimian, P.]]
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[[Category: Lima, C.D.]]
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[[Category: Lima, C D.]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Shen, V.]]
[[Category: Shen, V.]]
[[Category: G4P]]
[[Category: G4P]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:42:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:47 2008''

Revision as of 11:46, 21 February 2008

Image:1lnz.gif

1lnz, resolution 2.60Å

Drag the structure with the mouse to rotate

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.

About this Structure

1LNZ is a Single protein structure of sequence from Bacillus subtilis with and as ligands. 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

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