1mog: Difference between revisions
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[[Image:1mog.gif|left|200px]] | [[Image:1mog.gif|left|200px]] | ||
'''Crystal structure of H. salinarum dodecin''' | {{Structure | ||
|PDB= 1mog |SIZE=350|CAPTION= <scene name='initialview01'>1mog</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=RBF:RIBOFLAVINE'>RBF</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of H. salinarum dodecin''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MOG is a [ | 1MOG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOG OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum., Bieger B, Essen LO, Oesterhelt D, Structure. 2003 Apr;11(4):375-85. PMID:[http:// | Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum., Bieger B, Essen LO, Oesterhelt D, Structure. 2003 Apr;11(4):375-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12679016 12679016] | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: binding site for dimerized riboflavin]] | [[Category: binding site for dimerized riboflavin]] | ||
''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 12:46:06 2008'' | ||
Revision as of 13:46, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of H. salinarum dodecin
OverviewOverview
A novel, 68 amino acid long flavoprotein called dodecin has been discovered in the proteome of Halobacterium salinarum by inverse structural genomics. The 1.7 A crystal structure of this protein shows a dodecameric, hollow sphere-like arrangement of the protein subunits. Unlike other known flavoproteins, which bind only monomeric flavin cofactors, the structure of the dodecin oligomer comprises six riboflavin dimers. The dimerization of these riboflavins along the re-faces is mediated by aromatic, antiparallel pi staggering of their isoalloxazine moieties. A unique aromatic tetrade is formed by further sandwiching of the riboflavin dimers between the indole groups of two symmetry-related Trp36s. So far, the dodecins represent the smallest known flavoproteins. Based on the structure and the wide spread occurrences in pathogenic and soil eubacteria, a function in flavin storage or protection against radical or oxygenic stress is suggested for the dodecins.
About this StructureAbout this Structure
1MOG is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum., Bieger B, Essen LO, Oesterhelt D, Structure. 2003 Apr;11(4):375-85. PMID:12679016
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