2ccc: Difference between revisions
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[[Image:2ccc.gif|left|200px]] | [[Image:2ccc.gif|left|200px]] | ||
'''COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS''' | {{Structure | ||
|PDB= 2ccc |SIZE=350|CAPTION= <scene name='initialview01'>2ccc</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=LFN:LUMIFLAVIN'>LFN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CCC is a [ | 2CCC 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=2CCC OCA]. | ||
==Reference== | ==Reference== | ||
Dodecins: a family of lumichrome binding proteins., Grininger M, Zeth K, Oesterhelt D, J Mol Biol. 2006 Mar 31;357(3):842-57. Epub 2006 Jan 18. PMID:[http:// | Dodecins: a family of lumichrome binding proteins., Grininger M, Zeth K, Oesterhelt D, J Mol Biol. 2006 Mar 31;357(3):842-57. Epub 2006 Jan 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16460756 16460756] | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
''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 16:13:40 2008'' | ||
Revision as of 17:13, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS
OverviewOverview
Dodecin is a small dodecameric flavoprotein from Halobacterium salinarum that contains two flavins stacked between two tryptophan residues to form an aromatic tetrade. The functional properties of heterologously expressed dodecin were investigated by fluorescence spectroscopy, which allowed the determination of dissociation constants for a number of protein-ligand complexes. The values obtained were in the nanomolar to micromolar range and correlate positively with the ligand size. These data were supplemented by X-ray crystal structures of the apododecin and holocomplexes with lumichrome, lumiflavin, riboflavin and FMN at resolutions between 1.55 to 1.95 A to unravel a gating mechanism as the structural basis for the preferential binding of the small ligands lumichrome and lumiflavin. The detailed analysis of the dodecin manifold for preferential binding of lumichrome and lumiflavin provides insight on a subatom level into a protein's strategy to gain selectivity for low molecular mass compounds by steric restrictions rather than specific interactions. Investigations on the ligand composition of a wild-type dodecin crystal (1.32 A resolution) support conclusions of functional and structural investigations on heterologously expressed dodecin, and strongly suggest that lumichrome, a molecule associated with the flavin metabolism, is a ligand of dodecin in vivo. Studies on mutant protein and a Halorhodospira halophila homologue spread the idea of a lumichrome binding system as a possible "waste"-trapping device, widely distributed in prokaryotes.
About this StructureAbout this Structure
2CCC is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
ReferenceReference
Dodecins: a family of lumichrome binding proteins., Grininger M, Zeth K, Oesterhelt D, J Mol Biol. 2006 Mar 31;357(3):842-57. Epub 2006 Jan 18. PMID:16460756
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