1lnz
From Proteopedia
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| - | [[Image:1lnz.gif|left|200px]] | + | [[Image:1lnz.gif|left|200px]] |
| - | + | ||
| - | '''Structure of the Obg GTP-binding protein''' | + | {{Structure |
| + | |PDB= 1lnz |SIZE=350|CAPTION= <scene name='initialview01'>1lnz</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=G4P:GUANOSINE-5',3'-TETRAPHOSPHATE'>G4P</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of the Obg GTP-binding protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LNZ is a [ | + | 1LNZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LNZ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12429099 12429099] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: stress response]] | [[Category: stress response]] | ||
[[Category: stringent factor]] | [[Category: stringent factor]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:33:02 2008'' |
Revision as of 10:33, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 12:33:02 2008
Categories: Bacillus subtilis | Single protein | Buglino, J. | Burley, S K. | Hakimian, P. | Lima, C D. | NYSGXRC, New York Structural GenomiX Research Consortium. | Shen, V. | G4P | MG | Gtpase | Large g-protein | New york structural genomix research consortium | Nysgxrc | Obg | Protein structure initiative | Psi | Sporulation | Stress response | Stringent factor | Structural genomic
