2ccc: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:2ccc.gif|left|200px]]
[[Image:2ccc.gif|left|200px]]


{{Structure
<!--
|PDB= 2ccc |SIZE=350|CAPTION= <scene name='initialview01'>2ccc</scene>, resolution 1.70&Aring;
The line below this paragraph, containing "STRUCTURE_2ccc", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LFN:LUMIFLAVIN'>LFN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE=
-->
|DOMAIN=
{{STRUCTURE_2ccc| PDB=2ccc  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccc OCA], [http://www.ebi.ac.uk/pdbsum/2ccc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ccc RCSB]</span>
}}


'''COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS'''
'''COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS'''
Line 28: Line 25:
[[Category: Oesterhelt, D.]]
[[Category: Oesterhelt, D.]]
[[Category: Zeth, K.]]
[[Category: Zeth, K.]]
[[Category: flavoprotein]]
[[Category: Flavoprotein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:46:40 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:19:30 2008''

Revision as of 21:46, 3 May 2008

File:2ccc.gif

Template:STRUCTURE 2ccc

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 Page seeded by OCA on Sat May 3 21:46:40 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA