1n1q: Difference between revisions
New page: left|200px<br /><applet load="1n1q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n1q, resolution 2.20Å" /> '''Crystal structure of... |
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[[Image:1n1q.jpg|left|200px]]<br /><applet load="1n1q" size=" | [[Image:1n1q.jpg|left|200px]]<br /><applet load="1n1q" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1n1q, resolution 2.20Å" /> | caption="1n1q, resolution 2.20Å" /> | ||
'''Crystal structure of a Dps protein from Bacillus brevis'''<br /> | '''Crystal structure of a Dps protein from Bacillus brevis'''<br /> | ||
==Overview== | ==Overview== | ||
The crystallization of cellular components represents a unique survival | The crystallization of cellular components represents a unique survival strategy for bacterial cells under stressed conditions. A highly ordered, layered structure is often formed in such a process, which may involve one or more than one type of bio-macromolecules. The main advantage of biocrystallization has been attributed to the fact that it is a physical process and thus is independent of energy consumption. Dps is a protein that crystallizes to form a multi-layered structure in starved cells in order to protect DNA against oxidative damage and other detrimental factors. The multi-layered crystal structure of a Dps protein from Bacillus brevis has been revealed for the first time at atomic resolution in the absence of DNA. Inspection of the structure provides the first direct evidence for the existence of a di-nuclear ferroxidase center, which possesses unique features among all the di-iron proteins identified so far. It constitutes the structural basis for the ferroxidase activity of Dps in the crystalline state as well as in solution. This finding proves that the enzymatic process of detoxification of metal ions, which may cause severe oxidative damage to DNA, is the other important aspect of the defense mechanism performed by Dps. In the multi-layered structure, Dps dodecamers are organized in a highly ordered manner. They adopt the classic form of hexagonal packing in each layer of the structure. Such arrangement results in reinforced structural features that would facilitate the attraction and absorption of metal ions from the environment. The highly ordered layered structure may provide an ideal basis for the accommodation of DNA between the layers so that it can be isolated and protected from harmful factors under stress conditions. | ||
==About this Structure== | ==About this Structure== | ||
1N1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis] with FEO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1N1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis] with <scene name='pdbligand=FEO:'>FEO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1Q OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:21 2008'' | ||
Revision as of 15:01, 21 February 2008
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Crystal structure of a Dps protein from Bacillus brevis
OverviewOverview
The crystallization of cellular components represents a unique survival strategy for bacterial cells under stressed conditions. A highly ordered, layered structure is often formed in such a process, which may involve one or more than one type of bio-macromolecules. The main advantage of biocrystallization has been attributed to the fact that it is a physical process and thus is independent of energy consumption. Dps is a protein that crystallizes to form a multi-layered structure in starved cells in order to protect DNA against oxidative damage and other detrimental factors. The multi-layered crystal structure of a Dps protein from Bacillus brevis has been revealed for the first time at atomic resolution in the absence of DNA. Inspection of the structure provides the first direct evidence for the existence of a di-nuclear ferroxidase center, which possesses unique features among all the di-iron proteins identified so far. It constitutes the structural basis for the ferroxidase activity of Dps in the crystalline state as well as in solution. This finding proves that the enzymatic process of detoxification of metal ions, which may cause severe oxidative damage to DNA, is the other important aspect of the defense mechanism performed by Dps. In the multi-layered structure, Dps dodecamers are organized in a highly ordered manner. They adopt the classic form of hexagonal packing in each layer of the structure. Such arrangement results in reinforced structural features that would facilitate the attraction and absorption of metal ions from the environment. The highly ordered layered structure may provide an ideal basis for the accommodation of DNA between the layers so that it can be isolated and protected from harmful factors under stress conditions.
About this StructureAbout this Structure
1N1Q is a Single protein structure of sequence from Brevibacillus brevis with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The multi-layered structure of Dps with a novel di-nuclear ferroxidase center., Ren B, Tibbelin G, Kajino T, Asami O, Ladenstein R, J Mol Biol. 2003 Jun 6;329(3):467-77. PMID:12767829
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